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For: Ngo M, Ridgway ND. Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function. Mol Biol Cell 2009;20:1388-99. [PMID: 19129476 DOI: 10.1091/mbc.e08-09-0905] [Citation(s) in RCA: 141] [Impact Index Per Article: 8.8] [Reference Citation Analysis] [What about the content of this article? (0)] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/30/2022] Open

For:	Ngo M, Ridgway ND. Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function. Mol Biol Cell 2009;20:1388-99. [PMID: 19129476 DOI: 10.1091/mbc.e08-09-0905] [Citation(s) in RCA: 141] [Impact Index Per Article: 8.8] [Reference Citation Analysis] [What about the content of this article? (0)] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/30/2022] Open

Number

Cited by Other Article(s)

De Matteis MA, Fico M, Venditti R. Regulation and function of PI4P at the Golgi complex. Biochim Biophys Acta Mol Cell Biol Lipids 2025;1870:159626. [PMID: 40350028 DOI: 10.1016/j.bbalip.2025.159626] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/10/2025] [Revised: 05/07/2025] [Accepted: 05/08/2025] [Indexed: 05/14/2025]

Chen T, Li X, Hou P, He H, Wang H. VAPA suppresses BEFV and VSV-induced type I IFNs signaling response by targeting JAK1 for NEDD4-mediated ubiquitin-proteasome degradation. Vet Microbiol 2025;304:110456. [PMID: 40080976 DOI: 10.1016/j.vetmic.2025.110456] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/14/2024] [Revised: 03/03/2025] [Accepted: 03/03/2025] [Indexed: 03/15/2025]

Chen J, Chen Z, Sun T, Jiang E, Liu K, Nong Y, Yuan T, Dai CC, Yan Y, Ge J, Wu H, Yang T, Wang S, Su Z, Song T, Abdelbsset-Ismail A, Li Y, Li C, Singhal RA, Yang K, Cai L, Carll AP. Cell Function Graphics: TOGGLE delineates fate and function within individual cell types via single-cell transcriptomics. BIORXIV : THE PREPRINT SERVER FOR BIOLOGY 2025:2025.01.01.631041. [PMID: 40060433 PMCID: PMC11888173 DOI: 10.1101/2025.01.01.631041] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 04/02/2025]

Kodama TS, Furuita K, Kojima C. Beyond Static Tethering at Membrane Contact Sites: Structural Dynamics and Functional Implications of VAP Proteins. Molecules 2025;30:1220. [PMID: 40141996 PMCID: PMC11944328 DOI: 10.3390/molecules30061220] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/31/2024] [Revised: 02/22/2025] [Accepted: 02/28/2025] [Indexed: 03/28/2025] Open

Tamhankar PM, Kachhadiya T, Tamhankar V, Menon PG, Vaniawala S, Mithbawkar SM. The First Known Case Report of a Novel Homozygous Nonsense Variant in the OSBPL9 Gene Associated With Fetal Cerebral Ventriculomegaly, Cerebellar Hypoplasia, and Arthrogryposis Multiplex. Cureus 2025;17:e80010. [PMID: 40182349 PMCID: PMC11966592 DOI: 10.7759/cureus.80010] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Accepted: 03/04/2025] [Indexed: 04/05/2025] Open

Abstract

Oxysterol-binding protein-like protein 9 (OSBPL9) is a member of a large eukaryotic gene lipid transport protein family that mediates the exchange of sterols and phospholipids between the trans-Golgi network and the endoplasmic reticulum. Denovo missense mutations in the OSBPL9 gene have been previously reported to be associated with intellectual disability. Herein, we report for the first time, to the best of our knowledge, a novel homozygous nonsense variant in the OSBPL9 gene in a consanguineous family with two fetuses with cerebral ventriculomegaly, cerebellar hypoplasia, and arthrogryposis multiplex. Whole exome sequencing and homozygosity mapping by chromosomal microarray identified one fetus to be homozygous for a novel nonsense variant chr1-51760720C>CAAT or c.615_616insTAA or p.Pro206*. Exome sequencing identified the asymptomatic parents as carriers for the same variant, indicating an autosomal recessive inheritance pattern. A review of medical literature using databases such as PubMed/MEDLINE (Medical Literature Analysis and Retrieval System Online), and Google Scholar did not reveal any case with the OSBPL9 variant and fetal malformations such as ventriculomegaly, cerebellar hypoplasia, and arthrogryposis multiplex. A protein network analysis using the STRING (Search Tool for Retrieval of Interacting Genes/Proteins) database showed close interactions between the OSPBPL9, OSBP, PI4K2A, PIP5K1C, PI4KA, CERT1, EXOSC3, RARS2, VRK1, and TSEN54 genes but no interactions with the L1CAM, KIDINS220, and KIAA1109 genes. These proteins are important for the metabolism of sphingomyelin, sterol, and lipids such as phosphatidylinositol and ceramide in the cell. Mutations in these proteins are known to cause related genetic disorders, which include structural brain abnormalities, fetal arthrogryposis, and intellectual disability as a phenotype. This is the first known report of a homozygous variant in the OSBPL9 gene in a recessive inheritance pattern, and the first report of association with a fetal anomaly phenotype. Previously, only two cases with an OSBPL9 gene variant have been documented in the literature, showing a sporadic autosomal dominant inheritance pattern. Thus, this case report expands the phenotype of OSBPL9 gene-related human disease. This case report will aid clinical diagnosis, genetic counseling, and preventive strategies such as prenatal diagnosis and/or preimplantation genetic diagnosis in families affected with OSBPL9 gene variants. The limitation of this study is the lack of RNA, protein, cellular, or animal model studies or functional studies to confirm this association.

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Cunningham JL, Liu HY, Francisco J, Frietze KK, Corbalan JJ, Nickels JT. The sterol-regulating human ARV1 binds cholesterol and phospholipids through its conserved ARV1 homology domain. J Biol Chem 2025;301:108306. [PMID: 39952408 PMCID: PMC11952846 DOI: 10.1016/j.jbc.2025.108306] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/06/2024] [Revised: 01/31/2025] [Accepted: 02/05/2025] [Indexed: 02/17/2025] Open

Hamaï A, Drin G. Specificity of lipid transfer proteins: An in vitro story. Biochimie 2024;227:85-110. [PMID: 39304019 DOI: 10.1016/j.biochi.2024.09.007] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/04/2024] [Revised: 09/06/2024] [Accepted: 09/17/2024] [Indexed: 09/22/2024]

Duncan RS, Keightley A, Lopez AA, Hall CW, Koulen P. Proteomics Analysis on the Effects of Oxidative Stress and Antioxidants on Proteins Involved in Sterol Transport and Metabolism in Human Telomerase Transcriptase-Overexpressing-Retinal Pigment Epithelium Cells. Int J Mol Sci 2024;25:10893. [PMID: 39456672 PMCID: PMC11507349 DOI: 10.3390/ijms252010893] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 07/26/2024] [Revised: 09/16/2024] [Accepted: 10/01/2024] [Indexed: 10/28/2024] Open

Becker AP, Biletch E, Kennelly JP, Julio AR, Villaneuva M, Nagari RT, Turner DW, Burton NR, Fukuta T, Cui L, Xiao X, Hong SG, Mack JJ, Tontonoz P, Backus KM. Lipid- and protein-directed photosensitizer proximity labeling captures the cholesterol interactome. BIORXIV : THE PREPRINT SERVER FOR BIOLOGY 2024:2024.08.20.608660. [PMID: 39229057 PMCID: PMC11370482 DOI: 10.1101/2024.08.20.608660] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Grants] [Track Full Text] [Download PDF] [Subscribe] [Scholar Register] [Indexed: 09/05/2024]

Affiliation(s)

Andrew P. Becker Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
Elijah Biletch Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
John Paul Kennelly Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, UCLA, Los Angeles, Los Angeles, California 90095, USA
Ashley R. Julio Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
Miranda Villaneuva Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA Molecular Biology Institute, UCLA, Los Angeles, California 90095, USA
Rohith T. Nagari Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, UCLA, Los Angeles, Los Angeles, California 90095, USA Molecular Biology Institute, UCLA, Los Angeles, California 90095, USA
Daniel W. Turner Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
Nikolas R. Burton Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
Tomoyuki Fukuta Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan
Liujuan Cui Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, UCLA, Los Angeles, Los Angeles, California 90095, USA
Xu Xiao Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, UCLA, Los Angeles, Los Angeles, California 90095, USA
Soon-Gook Hong Molecular Biology Institute, UCLA, Los Angeles, California 90095, USA Division of Cardiology, Department of Medicine, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA
Julia J. Mack Molecular Biology Institute, UCLA, Los Angeles, California 90095, USA Division of Cardiology, Department of Medicine, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA
Peter Tontonoz Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, UCLA, Los Angeles, Los Angeles, California 90095, USA
Keriann M. Backus Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA Molecular Biology Institute, UCLA, Los Angeles, California 90095, USA Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, UCLA, Los Angeles, California 90095, USA Jonsson Cancer Center, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, USA UCLA-DOE Institute for Genomics and Proteomics, UCLA, Los Angeles, California 90095, USA

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Han Y, Liu X, Xu L, Wei Z, Gu Y, Ren Y, Hua W, Zhang Y, Liu X, Jiang C, Zhuang R, Hong W, Wang T. RILP Induces Cholesterol Accumulation in Lysosomes by Inhibiting Endoplasmic Reticulum-Endolysosome Interactions. Cells 2024;13:1313. [PMID: 39195203 PMCID: PMC11352460 DOI: 10.3390/cells13161313] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/03/2024] [Revised: 07/26/2024] [Accepted: 07/28/2024] [Indexed: 08/29/2024] Open

Affiliation(s)

Yang Han State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Xiaoqing Liu State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Liju Xu State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Ziheng Wei State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Yueting Gu State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Yandan Ren State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Wenyi Hua State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Yongtao Zhang State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Xiaoxi Liu State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Cong Jiang State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Ruijuan Zhuang State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)
Wanjin Hong State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.) Institute of Molecular and Cell Biology, A*STAR (Agency of Science, Technology and Research), Singapore 138673, Singapore
Tuanlao Wang State Key Laboratory of Cellular Stress Biology, School of Pharmaceutical Sciences, Fujian Provincial Key Laboratory of Innovative Drug Target Research, Xiamen University, Xiamen 361102, China; (Y.H.); (X.L.); (L.X.); (Z.W.); (Y.G.); (Y.R.); (W.H.); (Y.Z.); (X.L.); (C.J.); (R.Z.)

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Li JQ, Zhang J, Chen Y, Le T, Chang MX. Coordination of oxysterol binding protein 1 and VAP-A/B modulates the generation of cholesterol and viral inclusion bodies to promote grass carp reovirus replication. Front Immunol 2024;15:1419321. [PMID: 39081319 PMCID: PMC11286474 DOI: 10.3389/fimmu.2024.1419321] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 04/18/2024] [Accepted: 07/04/2024] [Indexed: 08/02/2024] Open

Ajiki M, Yoshikawa M, Miyazaki T, Kawasaki A, Aoki K, Nakatsu F, Tsukiji S. ORP9-PH domain-based fluorescent reporters for visualizing phosphatidylinositol 4-phosphate dynamics in living cells. RSC Chem Biol 2024;5:544-555. [PMID: 38846081 PMCID: PMC11151866 DOI: 10.1039/d3cb00232b] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/13/2023] [Accepted: 04/15/2024] [Indexed: 06/09/2024] Open

Sun S, Zhao G, Jia M, Jiang Q, Li S, Wang H, Li W, Wang Y, Bian X, Zhao YG, Huang X, Yang G, Cai H, Pastor-Pareja JC, Ge L, Zhang C, Hu J. Stay in touch with the endoplasmic reticulum. SCIENCE CHINA. LIFE SCIENCES 2024;67:230-257. [PMID: 38212460 DOI: 10.1007/s11427-023-2443-9] [Citation(s) in RCA: 21] [Impact Index Per Article: 21.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Received: 03/19/2023] [Accepted: 08/28/2023] [Indexed: 01/13/2024]

Affiliation(s)

Sha Sun National Laboratory of Biomacromolecules, Institute of Biophysics, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing, 100101, China
Gan Zhao The Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing, 100871, China
Mingkang Jia The Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing, 100871, China
Qing Jiang The Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing, 100871, China
Shulin Li State Key Laboratory of Membrane Biology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China
Haibin Wang National Laboratory of Biomacromolecules, Institute of Biophysics, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing, 100101, China
Wenjing Li Laboratory of Computational Biology & Machine Intelligence, School of Artificial Intelligence, University of Chinese Academy of Sciences, Beijing, 100049, China
Yunyun Wang State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China
Xin Bian State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China.
Yan G Zhao Brain Research Center, Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.
Xun Huang State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Innovation Academy for Seed Design, Chinese Academy of Sciences, Beijing, 100101, China.
Ge Yang Laboratory of Computational Biology & Machine Intelligence, School of Artificial Intelligence, University of Chinese Academy of Sciences, Beijing, 100049, China.
Huaqing Cai National Laboratory of Biomacromolecules, Institute of Biophysics, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing, 100101, China.
Jose C Pastor-Pareja State Key Laboratory of Membrane Biology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China. Institute of Neurosciences, Consejo Superior de Investigaciones Cientfflcas-Universidad Miguel Hernandez, San Juan de Alicante, 03550, Spain.
Liang Ge State Key Laboratory of Membrane Biology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Chuanmao Zhang The Ministry of Education Key Laboratory of Cell Proliferation and Differentiation, College of Life Sciences, Peking University, Beijing, 100871, China.
Junjie Hu National Laboratory of Biomacromolecules, Institute of Biophysics, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing, 100101, China.

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Naito T, Yang H, Koh DHZ, Mahajan D, Lu L, Saheki Y. Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites. Nat Commun 2023;14:5867. [PMID: 37735529 PMCID: PMC10514280 DOI: 10.1038/s41467-023-41213-w] [Citation(s) in RCA: 17] [Impact Index Per Article: 8.5] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/06/2023] [Accepted: 08/28/2023] [Indexed: 09/23/2023] Open

Yang H, Tan JX. Lysosomal quality control: molecular mechanisms and therapeutic implications. Trends Cell Biol 2023;33:749-764. [PMID: 36717330 PMCID: PMC10374877 DOI: 10.1016/j.tcb.2023.01.001] [Citation(s) in RCA: 42] [Impact Index Per Article: 21.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/15/2022] [Revised: 01/08/2023] [Accepted: 01/10/2023] [Indexed: 01/29/2023]

Iyer DR, Venkatraman J, Tanguy E, Vitale N, Mahapatra NR. Chromogranin A and its derived peptides: potential regulators of cholesterol homeostasis. Cell Mol Life Sci 2023;80:271. [PMID: 37642733 PMCID: PMC11072126 DOI: 10.1007/s00018-023-04908-3] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/03/2023] [Revised: 08/02/2023] [Accepted: 08/03/2023] [Indexed: 08/31/2023]

Vormittag S, Ende RJ, Derré I, Hilbi H. Pathogen vacuole membrane contact sites - close encounters of the fifth kind. MICROLIFE 2023;4:uqad018. [PMID: 37223745 PMCID: PMC10117887 DOI: 10.1093/femsml/uqad018] [Citation(s) in RCA: 5] [Impact Index Per Article: 2.5] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Figures] [Subscribe] [Scholar Register] [Received: 02/14/2023] [Revised: 03/30/2023] [Accepted: 04/06/2023] [Indexed: 05/25/2023]

Fang R, Jiang Q, Jia X, Jiang Z. ARMH3-mediated recruitment of PI4KB directs Golgi-to-endosome trafficking and activation of the antiviral effector STING. Immunity 2023;56:500-515.e6. [PMID: 36921576 DOI: 10.1016/j.immuni.2023.02.004] [Citation(s) in RCA: 35] [Impact Index Per Article: 17.5] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 09/15/2022] [Revised: 11/30/2022] [Accepted: 01/26/2023] [Indexed: 03/15/2023]

He R, Liu F, Wang H, Huang S, Xu K, Zhang C, Liu Y, Yu H. ORP9 and ORP10 form a heterocomplex to transfer phosphatidylinositol 4-phosphate at ER-TGN contact sites. Cell Mol Life Sci 2023;80:77. [PMID: 36853333 PMCID: PMC11072704 DOI: 10.1007/s00018-023-04728-5] [Citation(s) in RCA: 6] [Impact Index Per Article: 3.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/17/2022] [Revised: 02/15/2023] [Accepted: 02/15/2023] [Indexed: 03/01/2023]

Singh RP, Poh YP, Sinha SD, Wideman JG. Evolutionary History of Oxysterol-Binding Proteins Reveals Complex History of Duplication and Loss in Animals and Fungi. CONTACT (THOUSAND OAKS (VENTURA COUNTY, CALIF.)) 2023;6:25152564221150428. [PMID: 37366416 PMCID: PMC10243569 DOI: 10.1177/25152564221150428] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Figures] [Subscribe] [Scholar Register] [Received: 06/14/2022] [Revised: 12/17/2022] [Accepted: 12/21/2022] [Indexed: 06/28/2023]

Balla T, Gulyas G, Mandal A, Alvarez-Prats A, Niu Y, Kim YJ, Pemberton J. Roles of Phosphatidylinositol 4-Phosphorylation in Non-vesicular Cholesterol Trafficking. ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY 2023;1422:327-352. [PMID: 36988887 PMCID: PMC11135459 DOI: 10.1007/978-3-031-21547-6_12] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 03/30/2023]

Arita M. Essential Domains of Oxysterol-Binding Protein Required for Poliovirus Replication. Viruses 2022;14:v14122672. [PMID: 36560676 PMCID: PMC9786093 DOI: 10.3390/v14122672] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/28/2022] [Revised: 11/25/2022] [Accepted: 11/28/2022] [Indexed: 12/05/2022] Open

Wenzel EM, Elfmark LA, Stenmark H, Raiborg C. ER as master regulator of membrane trafficking and organelle function. J Cell Biol 2022;221:e202205135. [PMID: 36108241 PMCID: PMC9481738 DOI: 10.1083/jcb.202205135] [Citation(s) in RCA: 59] [Impact Index Per Article: 19.7] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/30/2022] [Revised: 08/16/2022] [Accepted: 08/22/2022] [Indexed: 12/13/2022] Open

Tan JX, Finkel T. A phosphoinositide signalling pathway mediates rapid lysosomal repair. Nature 2022;609:815-821. [PMID: 36071159 PMCID: PMC9450835 DOI: 10.1038/s41586-022-05164-4] [Citation(s) in RCA: 179] [Impact Index Per Article: 59.7] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/18/2020] [Accepted: 07/29/2022] [Indexed: 12/23/2022]

Depta L, Whitmarsh-Everiss T, Laraia L. Structure, function and small molecule modulation of intracellular sterol transport proteins. Bioorg Med Chem 2022;68:116856. [PMID: 35716590 DOI: 10.1016/j.bmc.2022.116856] [Citation(s) in RCA: 7] [Impact Index Per Article: 2.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/09/2022] [Accepted: 05/23/2022] [Indexed: 11/02/2022]

The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals. MEMBRANES 2022;12:membranes12070696. [PMID: 35877899 PMCID: PMC9324892 DOI: 10.3390/membranes12070696] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Subscribe] [Scholar Register] [Received: 05/11/2022] [Revised: 07/04/2022] [Accepted: 07/05/2022] [Indexed: 01/27/2023]

Kobayashi J, Arita M, Sakai S, Kojima H, Senda M, Senda T, Hanada K, Kato R. Ligand Recognition by the Lipid Transfer Domain of Human OSBP Is Important for Enterovirus Replication. ACS Infect Dis 2022;8:1161-1170. [PMID: 35613096 DOI: 10.1021/acsinfecdis.2c00108] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/14/2022]

Arora A, Taskinen JH, Olkkonen VM. Coordination of inter-organelle communication and lipid fluxes by OSBP-related proteins. Prog Lipid Res 2022;86:101146. [PMID: 34999137 DOI: 10.1016/j.plipres.2022.101146] [Citation(s) in RCA: 22] [Impact Index Per Article: 7.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/01/2021] [Revised: 12/10/2021] [Accepted: 01/03/2022] [Indexed: 12/31/2022]

Kawasaki A, Sakai A, Nakanishi H, Hasegawa J, Taguchi T, Sasaki J, Arai H, Sasaki T, Igarashi M, Nakatsu F. PI4P/PS countertransport by ORP10 at ER-endosome membrane contact sites regulates endosome fission. J Cell Biol 2022;221:212876. [PMID: 34817532 PMCID: PMC8624802 DOI: 10.1083/jcb.202103141] [Citation(s) in RCA: 35] [Impact Index Per Article: 11.7] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/22/2021] [Revised: 09/28/2021] [Accepted: 10/25/2021] [Indexed: 12/17/2022] Open

Kors S, Costello JL, Schrader M. VAP Proteins - From Organelle Tethers to Pathogenic Host Interactors and Their Role in Neuronal Disease. Front Cell Dev Biol 2022;10:895856. [PMID: 35756994 PMCID: PMC9213790 DOI: 10.3389/fcell.2022.895856] [Citation(s) in RCA: 21] [Impact Index Per Article: 7.0] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/14/2022] [Accepted: 04/25/2022] [Indexed: 12/26/2022] Open

Nakatsu F, Kawasaki A. Functions of Oxysterol-Binding Proteins at Membrane Contact Sites and Their Control by Phosphoinositide Metabolism. Front Cell Dev Biol 2021;9:664788. [PMID: 34249917 PMCID: PMC8264513 DOI: 10.3389/fcell.2021.664788] [Citation(s) in RCA: 42] [Impact Index Per Article: 10.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/06/2021] [Accepted: 05/06/2021] [Indexed: 01/10/2023] Open

Baggen J, Persoons L, Vanstreels E, Jansen S, Van Looveren D, Boeckx B, Geudens V, De Man J, Jochmans D, Wauters J, Wauters E, Vanaudenaerde BM, Lambrechts D, Neyts J, Dallmeier K, Thibaut HJ, Jacquemyn M, Maes P, Daelemans D. Genome-wide CRISPR screening identifies TMEM106B as a proviral host factor for SARS-CoV-2. Nat Genet 2021;53:435-444. [PMID: 33686287 DOI: 10.1038/s41588-021-00805-2] [Citation(s) in RCA: 157] [Impact Index Per Article: 39.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/02/2020] [Accepted: 01/27/2021] [Indexed: 01/31/2023]

Affiliation(s)

Jim Baggen KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium.
Leentje Persoons KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Els Vanstreels KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Sander Jansen KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Dominique Van Looveren KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium.,KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Translational Platform Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Bram Boeckx KU Leuven Department of Human Genetics, Laboratory for Translational Genetics, Leuven, Belgium.,VIB Center for Cancer Biology, VIB, Leuven, Belgium
Vincent Geudens KU Leuven Department of Chronic Diseases and Metabolism, Laboratory of Respiratory Diseases and Thoracic Surgery (BREATHE), Leuven, Belgium
Julie De Man KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Dirk Jochmans KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Joost Wauters KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Clinical Infectious and Inflammatory Disorders, Leuven, Belgium
Els Wauters KU Leuven Department of Chronic Diseases and Metabolism, Laboratory of Respiratory Diseases and Thoracic Surgery (BREATHE), Leuven, Belgium
Bart M Vanaudenaerde KU Leuven Department of Chronic Diseases and Metabolism, Laboratory of Respiratory Diseases and Thoracic Surgery (BREATHE), Leuven, Belgium
Diether Lambrechts KU Leuven Department of Human Genetics, Laboratory for Translational Genetics, Leuven, Belgium.,VIB Center for Cancer Biology, VIB, Leuven, Belgium
Johan Neyts KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Kai Dallmeier KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Hendrik Jan Thibaut KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium.,KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Translational Platform Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Maarten Jacquemyn KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium
Piet Maes KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Clinical and Epidemiological Virology, Rega Institute, Leuven, Belgium
Dirk Daelemans KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven, Belgium.

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The emerging roles of OSBP-related proteins in cancer: Impacts through phosphoinositide metabolism and protein-protein interactions. Biochem Pharmacol 2021;196:114455. [PMID: 33556339 DOI: 10.1016/j.bcp.2021.114455] [Citation(s) in RCA: 12] [Impact Index Per Article: 3.0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/06/2021] [Revised: 01/26/2021] [Accepted: 01/28/2021] [Indexed: 01/04/2023]

David Y, Castro IG, Schuldiner M. The Fast and the Furious: Golgi Contact Sites. CONTACT (THOUSAND OAKS (VENTURA COUNTY, CALIF.)) 2021;4:1-15. [PMID: 35071979 PMCID: PMC7612241 DOI: 10.1177/25152564211034424] [Citation(s) in RCA: 10] [Impact Index Per Article: 2.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Subscribe] [Scholar Register] [Indexed: 11/25/2022]

Corbeil D, Santos MF, Karbanová J, Kurth T, Rappa G, Lorico A. Uptake and Fate of Extracellular Membrane Vesicles: Nucleoplasmic Reticulum-Associated Late Endosomes as a New Gate to Intercellular Communication. Cells 2020;9:cells9091931. [PMID: 32825578 PMCID: PMC7563309 DOI: 10.3390/cells9091931] [Citation(s) in RCA: 57] [Impact Index Per Article: 11.4] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 07/31/2020] [Revised: 08/18/2020] [Accepted: 08/20/2020] [Indexed: 02/06/2023] Open

Delfosse V, Bourguet W, Drin G. Structural and Functional Specialization of OSBP-Related Proteins. ACTA ACUST UNITED AC 2020. [DOI: 10.1177/2515256420946627] [Citation(s) in RCA: 12] [Impact Index Per Article: 2.4] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/08/2023]

Silva BSC, DiGiovanni L, Kumar R, Carmichael RE, Kim PK, Schrader M. Maintaining social contacts: The physiological relevance of organelle interactions. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH 2020;1867:118800. [PMID: 32712071 PMCID: PMC7377706 DOI: 10.1016/j.bbamcr.2020.118800] [Citation(s) in RCA: 46] [Impact Index Per Article: 9.2] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Figures] [Subscribe] [Scholar Register] [Received: 05/21/2020] [Revised: 07/12/2020] [Accepted: 07/19/2020] [Indexed: 02/07/2023]

Lipp NF, Ikhlef S, Milanini J, Drin G. Lipid Exchangers: Cellular Functions and Mechanistic Links With Phosphoinositide Metabolism. Front Cell Dev Biol 2020;8:663. [PMID: 32793602 PMCID: PMC7385082 DOI: 10.3389/fcell.2020.00663] [Citation(s) in RCA: 32] [Impact Index Per Article: 6.4] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/15/2020] [Accepted: 07/01/2020] [Indexed: 12/28/2022] Open

ER-Golgi membrane contact sites. Biochem Soc Trans 2020;48:187-197. [DOI: 10.1042/bst20190537] [Citation(s) in RCA: 20] [Impact Index Per Article: 4.0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/06/2019] [Revised: 01/20/2020] [Accepted: 01/24/2020] [Indexed: 12/13/2022]

Liu H, Huang S. Role of oxysterol-binding protein-related proteins in malignant human tumours. World J Clin Cases 2020;8:1-10. [PMID: 31970164 PMCID: PMC6962060 DOI: 10.12998/wjcc.v8.i1.1] [Citation(s) in RCA: 13] [Impact Index Per Article: 2.6] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 10/07/2019] [Revised: 12/11/2019] [Accepted: 12/13/2019] [Indexed: 02/05/2023] Open

Naito T, Ercan B, Krshnan L, Triebl A, Koh DHZ, Wei FY, Tomizawa K, Torta FT, Wenk MR, Saheki Y. Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex. eLife 2019;8:51401. [PMID: 31724953 PMCID: PMC6905856 DOI: 10.7554/elife.51401] [Citation(s) in RCA: 112] [Impact Index Per Article: 18.7] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/27/2019] [Accepted: 11/13/2019] [Indexed: 12/18/2022] Open

Abstract

Cholesterol is a major structural component of the plasma membrane (PM). The majority of PM cholesterol forms complexes with other PM lipids, making it inaccessible for intracellular transport. Transition of PM cholesterol between accessible and inaccessible pools maintains cellular homeostasis, but how cells monitor the accessibility of PM cholesterol remains unclear. We show that endoplasmic reticulum (ER)-anchored lipid transfer proteins, the GRAMD1s, sense and transport accessible PM cholesterol to the ER. GRAMD1s bind to one another and populate ER-PM contacts by sensing a transient expansion of the accessible pool of PM cholesterol via their GRAM domains. They then facilitate the transport of this cholesterol via their StART-like domains. Cells that lack all three GRAMD1s exhibit striking expansion of the accessible pool of PM cholesterol as a result of less efficient PM to ER transport of accessible cholesterol. Thus, GRAMD1s facilitate the movement of accessible PM cholesterol to the ER in order to counteract an acute increase of PM cholesterol, thereby activating non-vesicular cholesterol transport.

The human body contains trillions of cells. At the outer edge of each cell is the plasma membrane, which protects the cell from the external environment. This membrane is mostly made of fatty molecules known as lipids and about half of these lipids are specifically cholesterol. Human cells can either take up cholesterol that were obtained via the diet or produce it within a compartment of the cell called the endoplasmic reticulum.

Cells need to monitor the cholesterol levels in both the endoplasmic reticulum and the plasma membrane in order to regulate the uptake or production of this lipid. For example, if there is too much of cholesterol in the plasma membrane, then the cell transports some to the endoplasmic reticulum to tell it to shut down cholesterol production. However, how these different areas of the cell communicate with each other, and transport cholesterol, has remained unclear.

Naito et al. set out to look for key regulators of cholesterol transport and identified a group of endoplasmic reticulum proteins called GRAMD1 proteins. Cholesterol in the plasma membrane is either accessible or inaccessible, meaning it either can or cannot be moved back into the cell. The GRAMD1 proteins sense accessible cholesterol, and experiments with human cells grown in the laboratory showed that, specifically, the GRAMD1 proteins work together in a complex to sense accessible cholesterol at or near the plasma membrane. One particular part of the protein senses when the amount of accessible cholesterol reaches a certain level at the plasma membrane; when this threshold is reached, the complex flips a switch to start the transport of cholesterol to the endoplasmic reticulum and tell it to shut down cholesterol production.

This coupling of sensing and transporting lipids by one protein complex also helps maintain the right ratio of accessible and inaccessible cholesterol in the plasma membrane to prevent cells from activating unwanted cell-signaling events. Getting rid of the GRAMD1 proteins in cells, or removing sensing part of these proteins, leads to inefficient transport of cholesterol. A better understanding of how GRAMD1 proteins sense the accessibility of cholesterol could potentially help identify new approaches to control cholesterol transport inside cells. This may in turn eventually lead to new treatments that counteract the defects in cholesterol metabolism seen in some forms of neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease.

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Masone MC, Morra V, Venditti R. Illuminating the membrane contact sites between the endoplasmic reticulum and the trans-Golgi network. FEBS Lett 2019;593:3135-3148. [PMID: 31610025 DOI: 10.1002/1873-3468.13639] [Citation(s) in RCA: 9] [Impact Index Per Article: 1.5] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 08/08/2019] [Revised: 10/08/2019] [Accepted: 10/08/2019] [Indexed: 12/22/2022]

Arnal-Levron M, Chen Y, Greimel P, Calevro F, Gaget K, Riols F, Batut A, Bertrand-Michel J, Hullin-Matsuda F, Olkkonen VM, Delton I, Luquain-Costaz C. Bis(monoacylglycero)phosphate regulates oxysterol binding protein-related protein 11 dependent sterol trafficking. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:1247-1257. [DOI: 10.1016/j.bbalip.2019.05.011] [Citation(s) in RCA: 10] [Impact Index Per Article: 1.7] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/22/2018] [Revised: 05/21/2019] [Accepted: 05/23/2019] [Indexed: 02/06/2023]

The Great Escape: how phosphatidylinositol 4-kinases and PI4P promote vesicle exit from the Golgi (and drive cancer). Biochem J 2019;476:2321-2346. [DOI: 10.1042/bcj20180622] [Citation(s) in RCA: 34] [Impact Index Per Article: 5.7] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/16/2019] [Revised: 08/06/2019] [Accepted: 08/12/2019] [Indexed: 12/13/2022]

Nishimura T, Stefan CJ. Specialized ER membrane domains for lipid metabolism and transport. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1865:158492. [PMID: 31349025 DOI: 10.1016/j.bbalip.2019.07.001] [Citation(s) in RCA: 13] [Impact Index Per Article: 2.2] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 04/22/2019] [Revised: 07/02/2019] [Accepted: 07/03/2019] [Indexed: 11/15/2022]

Gillingham AK, Bertram J, Begum F, Munro S. In vivo identification of GTPase interactors by mitochondrial relocalization and proximity biotinylation. eLife 2019;8:45916. [PMID: 31294692 PMCID: PMC6639074 DOI: 10.7554/elife.45916] [Citation(s) in RCA: 65] [Impact Index Per Article: 10.8] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/08/2019] [Accepted: 07/10/2019] [Indexed: 12/11/2022] Open

Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae. Braz J Microbiol 2019;50:415-424. [PMID: 30848436 DOI: 10.1007/s42770-019-00060-y] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/11/2018] [Accepted: 11/06/2018] [Indexed: 01/03/2023] Open

Venditti R, Masone MC, Rega LR, Di Tullio G, Santoro M, Polishchuk E, Serrano IC, Olkkonen VM, Harada A, Medina DL, La Montagna R, De Matteis MA. The activity of Sac1 across ER-TGN contact sites requires the four-phosphate-adaptor-protein-1. J Cell Biol 2019;218:783-797. [PMID: 30659099 PMCID: PMC6400556 DOI: 10.1083/jcb.201812021] [Citation(s) in RCA: 68] [Impact Index Per Article: 11.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/05/2018] [Revised: 12/14/2018] [Accepted: 12/19/2018] [Indexed: 01/05/2023] Open

Venditti R, Rega LR, Masone MC, Santoro M, Polishchuk E, Sarnataro D, Paladino S, D'Auria S, Varriale A, Olkkonen VM, Di Tullio G, Polishchuk R, De Matteis MA. Molecular determinants of ER-Golgi contacts identified through a new FRET-FLIM system. J Cell Biol 2019;218:1055-1065. [PMID: 30659100 PMCID: PMC6400564 DOI: 10.1083/jcb.201812020] [Citation(s) in RCA: 91] [Impact Index Per Article: 15.2] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 12/05/2018] [Revised: 12/14/2018] [Accepted: 12/18/2018] [Indexed: 01/05/2023] Open

Koponen A, Arora A, Takahashi K, Kentala H, Kivelä AM, Jääskeläinen E, Peränen J, Somerharju P, Ikonen E, Viitala T, Olkkonen VM. ORP2 interacts with phosphoinositides and controls the subcellular distribution of cholesterol. Biochimie 2018;158:90-101. [PMID: 30590084 DOI: 10.1016/j.biochi.2018.12.013] [Citation(s) in RCA: 31] [Impact Index Per Article: 4.4] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/21/2018] [Accepted: 12/20/2018] [Indexed: 01/06/2023]