Activation of cytosolic Slingshot-1 phosphatase by gelsolin-generated soluble actin filaments

被引：5

作者：

Takahashi, Katsunori ^{[1
]}

Kanno, Shin-ichiro ^{[2
]}

Mizuno, Kensaku ^{[1
]}

机构：

[1] Tohoku Univ, Grad Sch Life Sci, Dept Biomol Sci, Sendai, Miyagi 9808578, Japan

[2] Tohoku Univ, Inst Dev Aging & Canc, Div Dynam Proteome Canc & Aging, Sendai, Miyagi 9808575, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2014年 / 454卷 / 03期

关键词：

Slingshot; Gelsolin; Cofilin; Scinderin; Actin oligomers; Phosphatase; COFILIN PHOSPHORYLATION; LIM-KINASE; REORGANIZATION; DEPHOSPHORYLATION; ADF/COFILIN; MECHANISMS; MOTILITY; DYNAMICS; FAMILY; ROLES;

D O I：

10.1016/j.bbrc.2014.10.108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Slingshot-1 (SSH1) is a protein phosphatase that dephosphorylates and activates cofilin, an actin-severing and -disassembling protein. SSH1 is bound to and activated by F-actin, but not G-actin. SSH1 is accumulated in the F-actin-rich lamellipodium but is also diffusely distributed in the cytoplasm. It remains unknown whether SSH1 is activated by soluble (low-level polymerized) actin filaments in the cytoplasm. In this study, we show that SSH1 binds to gelsolin via actin filaments in the cytosolic fraction. Gelsolin promoted solubilization of actin filaments and SSH1 in cell-free assays and in cultured cells. SSH1 was activated by gelsolin-generated soluble actin filaments. Furthermore, gelsolin enhanced coffin dephosphorylation in neuregulin-stimulated cells. Our results suggest that cytosolic SSH1 forms a complex with gelsolin via soluble actin filaments and is activated by gelsolin-generated soluble actin filaments and that gelsolin promotes stimulus-induced cofilin dephosphorylation through increasing soluble actin filaments, which support SSH1 activation in the cytoplasm. (C) 2014 Elsevier Inc. All rights reserved.

引用

页码：471 / 477

页数：7

共 33 条

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