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Phosphorylation on the Ser 824 residue of TRPV4 prefers to bind with F-actin than with microtubules to expand the cell surface area.

Abstract：

: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 Ser 824 residue of TRPV4 is phosphorylated by SGK1. 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, Ca(2+) influx, protein stability, and cell surface area (expansion of plasma membrane).

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Shin SH,Lee EJ,Hyun S,Chun J,Kim Y,Kang SS

doi

10.1016/j.cellsig.2011.11.002

subject

Has Abstract

pub_date

2012-03-01 00:00:00

pages

641-51

issue

3

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(11)00343-3

journal_volume

24

pub_type

杂志文章

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