Samuels AL, Louw A, Zareie R, Ingley E. Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ. World J Biol Chem 2017; 8(3): 163-174 [PMID: 28924458 DOI: 10.4331/wjbc.v8.i3.163]
Corresponding Author of This Article
Dr. Evan Ingley, Professor, Cell Signalling Group, School of Veterinary and Health Sciences, Murdoch University, 90 South Street, Murdoch, WA 6150, Australia. evan.ingley@mudcoh.edu.au
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Biochemistry & Molecular Biology
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Basic Study
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Aug 26, 2017 (publication date) through Feb 18, 2026
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World Journal of Biological Chemistry
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1949-8454
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Samuels AL, Louw A, Zareie R, Ingley E. Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ. World J Biol Chem 2017; 8(3): 163-174 [PMID: 28924458 DOI: 10.4331/wjbc.v8.i3.163]
World J Biol Chem. Aug 26, 2017; 8(3): 163-174 Published online Aug 26, 2017. doi: 10.4331/wjbc.v8.i3.163
Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ
Amy L Samuels, Alison Louw, Reza Zareie, Evan Ingley
Amy L Samuels, Alison Louw, Evan Ingley, Cell Signalling Group, Harry Perkins Institute of Medical Research and Centre for Medical Research, the University of Western Australia, Nedlands, WA 6009, Australia
Reza Zareie, Proteomics International Laboratories Ltd, Nedlands, WA 6009, Australia
Reza Zareie, Proteowa Pty Ltd, SABC, Murdoch University, Murdoch, WA 6150, Australia
Evan Ingley, Cell Signalling Group, School of Veterinary and Health Sciences, Murdoch University, Murdoch, WA 6150, Australia. evan.ingley@mudcoh.edu.au
Author contributions: Samuels AL and Louw A contributed equally to the manuscript and designed, supported and performed experiments, and analyzed data; Zareie R designed and performed experiments, and analysed data; Ingley E designed and supported the research, designed and undertook experiments, analyzed data and contributed to writing the manuscript.
Supported by the National Health and Medical Research Council, Nos. 403987, 513714 and 634352; the Medical Research Foundation of Royal Perth Hospital; and the Cancer Council of Western Australia; Evan Ingley received support from the Cancer Council of Western Australia, the Harry Perkins Institute of Medical Research; Sock-it-to-Sarcoma and the Hollywood Private Hospital Research Foundation; and the MACA Ride to Conquer Cancer.
Conflict-of-interest statement: Each author declares no conflict of interest.
Data sharing statement: All data are available upon request.
Correspondence to: Dr. Evan Ingley, Professor, Cell Signalling Group, School of Veterinary and Health Sciences, Murdoch University, 90 South Street, Murdoch, WA 6150, Australia. evan.ingley@mudcoh.edu.au
Telephone: +61-8-61510738 Fax: +61-8-61510701
Received: January 25, 2017 Peer-review started: February 1, 2017 First decision: March 8, 2017 Revised: April 28, 2017 Accepted: May 12, 2017 Article in press: May 15, 2017 Published online: August 26, 2017 Processing time: 209 Days and 18.3 Hours
Core Tip
Core tip: Ankrd54 is a nuclear-cytoplasmic shuttling adaptor that interacts with Lyn, Btk, Txk, and HCLS1. Activation of PKC kinases promoted nuclear export and phosphorylation of Ankrd54, and increased interaction and cytoplasmic co-localization with Lyn. Co-expression of an active form of the PKCδ isoform specifically promoted both phosphorylation and cytoplasmic localization of Ankrd54. Alanine mutation of several serine residues in the amino-terminal region of Ankrd54 reduced both phorbol 12-myristate 13-acetate induced cytoplasmic localization and phosphorylation of Ankrd54. These results identify PKCδ as a major regulator of nuclear-cytoplasmic shuttling and interaction of Ankrd54 with Lyn, through its phosphorylation of at least the Ser18 residue.
