Journal
CELLULAR SIGNALLING
Volume 24, Issue 3, Pages 641-651Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2011.11.002
Keywords
TRPV4; SGK1; Subcellular localization; F-actin; 4-alpha PDD
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Funding
- National Research Foundation of Korea (NRF) [2009-0076024, 2009-0069007]
- Korea government (MEST)
- National Research Foundation of Korea [2009-0069007, 351-2009-2-C00139, 2009-0076024] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Previously, we demonstrated that the transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is one of the serum glucocorticoid-induced protein kinase1 (SGK1) authentic substrate proteins, and that the Set 824 residue of TRPV4 is phosphorylated by SGK1 [1]. In this study, we demonstrated that phosphorylation on the Ser 824 residue of TRPV4 is required for its interaction with F-actin, using TRPV4 mutants (S824D; a phospho-mimicking TRPV4 mutant and S824A; a non-phosphorylatable TRPV4 mutant) and its proper subcellular localization. Additionally, we noted that the phosphorylation of the Ser824 residue promotes its single channel activity. Ca2+ influx, protein stability, and cell surface area (expansion of plasma membrane). (C) 2011 Elsevier Inc. All rights reserved.
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