AIP1/WDR1 supports mitotic cell rounding

被引：45

作者：

Fujibuchi, T

Abe, Y ^{[1
]}

Takeuchi, T

Imai, Y

Kamei, Y

Murase, R

Ueda, N

Shigemoto, K

Yamamoto, H

Kito, K

机构：

[1] Ehime Univ, Sch Med, Natl Univ Corp, Dept Pathol,Div Mol Pathol, Tohon, Ehime 7910295, Japan

[2] Ehime Univ, Sch Med, Natl Univ Corp, Dept Orthoped Surg, Tohon, Ehime 7910295, Japan

[3] Ehime Univ, Sch Med, Natl Univ Corp, Dept Environm Hlth,Div Ecogenet, Tohon, Ehime 7910295, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 327卷 / 01期

关键词：

actin turnover; mitotic cell rounding; cofilin; AIP1/WDR1;

D O I：

10.1016/j.bbrc.2004.11.156

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：

The actin cytoskeleton plays a fundamental role in configuring cell shapes and movements. Actin interacting protein 1 (AIP1)/ tryptophan-aspartate-repeat protein 1 (WDR1) induces actin severing and disassembly cooperating with ADF/cofilin. We found that mitotic cell flattening but not rounding was manifested by suppression of AIP1/WDR1 in cells. This mitotic cell flattening was not due to any changes in phosphorylation and distribution of cofilin in cells. We carried out a direct observation of actin filament severing/disassembly assay and found that phosphorylated cofilin still somewhat severs/disassembles actin filaments and that AIP1/WDR1 effaces this in vitro. We suggest that the phosphorylation of ADF/cofilin will be insufficient to completely inhibit actin turnover during mitosis, and that AIP1/WDR1 could abort the severing/disassembly activity somewhat still carried out due to phosphorylated ADF/cofilin. This mechanism could be required to induce cell morphologic changes, especially mitotic cell rounding. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：268 / 275

页数：8

共 31 条

[1] Cloning and expression of a novel MAPKK-like protein kinase, lymphokine-activated killer T-cell-originated protein kinase, specifically expressed in the testis and activated lymphoid cells [J].