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Articles Published Processes
8/23/2017 3:39:21 AM | Browse: 1119 | Download: 1806
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Received |
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2017-01-30 12:53 |
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Peer-Review Started |
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2017-02-01 20:18 |
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To Make the First Decision |
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2017-03-08 09:34 |
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Return for Revision |
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2017-03-09 15:05 |
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Revised |
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2017-04-28 12:02 |
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Second Decision |
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2017-05-07 18:44 |
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Accepted by Journal Editor-in-Chief |
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Accepted by Executive Editor-in-Chief |
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2017-05-15 05:45 |
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Articles in Press |
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2017-05-15 05:45 |
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Publication Fee Transferred |
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2017-05-18 06:29 |
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Edit the Manuscript by Language Editor |
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Typeset the Manuscript |
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2017-08-15 09:28 |
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Publish the Manuscript Online |
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2017-08-23 03:39 |
Category |
Biochemistry & Molecular Biology |
Manuscript Type |
Basic Study |
Article Title |
Control of nuclear-cytoplasmic shuttling of Ankrd54 by PKCδ
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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 |
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Evan Ingley received support from the Cancer Council of Western Australia, the Harry Perkins Institute of Medical Research |
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Sock-it-to-Sarcoma and the Hollywood Private Hospital Research Foundation |
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the MACA Ride to Conquer Cancer |
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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 |
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