Publication Name	World Journal of Biological Chemistry
Manuscript ID	32888
Country	Australia

Received	2017-01-30 12:53
Peer-Review Started	2017-02-01 20:18
First Decision by Editorial Office Director
Return for Revision	2017-03-09 15:05
Revised	2017-04-28 12:02
Publication Fee Transferred	2017-05-18 06:29
Second Decision by Editor	2017-05-07 18:44
Second Decision by Editor-in-Chief
Final Decision by Editorial Office Director	2017-05-15 05:45
Articles in Press	2017-05-15 05:45
Edit the Manuscript by Language Editor
Typeset the Manuscript	2017-08-15 09:28
Publish the Manuscript Online	2017-08-23 03:39

ISSN	1949-8454 (online)
Open Access
Copyright	© The Author(s) 2017. Published by Baishideng Publishing Group Inc. All rights reserved.
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Category	Biochemistry & Molecular Biology
Manuscript Type	Basic Study
Article Title	Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ
Manuscript Source	Unsolicited Manuscript
All Author List	Amy L Samuels, Alison Louw, Reza Zareie and Evan Ingley
Funding Agency and Grant Number	Funding Agency Grant Number the National Health and Medical Research Council 403987, 513714 and 634352 he 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 the MACA Ride to Conquer Cancer
Corresponding Author	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
Key Words	Ankrd54; PKCδ; Lyn; Btk; Phosphorylation
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.
Publish Date	2017-08-23 03:39
Citation	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
URL	http://www.wjgnet.com/1949-8454/full/v8/i3/163.htm
DOI	http://dx.doi.org/10.4331/wjbc.v8.i3.163

Full Article (PDF)	WJBC-8-163.pdf
Full Article (Word)	WJBC-8-163.doc
Manuscript File	32888-Review.docx
Answering Reviewers	32888-Answering reviewers.pdf
Audio Core Tip	32888-Audio core tip.aiff
Biostatistics Review Certificate	32888-Biostatistics statement.pdf
Conflict-of-Interest Disclosure Form	32888-Conflict-of-interest statement.pdf
Copyright License Agreement	32888-Copyright assignment.pdf
Institutional Animal Care and Use Committee Approval Form or Document	32888-Institutional animal care and use committee statement.pdf
Institutional Review Board Approval Form or Document	32888-Institutional review board statement.pdf
Peer-review Report	32888-Peer-review(s).pdf
Scientific Misconduct Check	32888-Scientific misconduct check.pdf
Scientific Editor Work List	32888-Scientific editor work list.pdf