FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex

被引：70

作者：

Ikenouchi, Junichi ^{[1
,2
]}

Umeda, Masato ^{[1
]}

机构：

[1] Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan

[2] Japan Sci & Technol Agcy, Precursory Res Embryon Sci & Technol, Kawaguchi, Saitama 3320012, Japan

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2010年 / 107卷 / 02期

基金：

日本科学技术振兴机构;

关键词：

adherens junction; tight junction; cell polarity; epithelial cells; cytohesin; EXCHANGE FACTOR; E-CADHERIN; ADHERENS JUNCTIONS; TIGHT JUNCTION; CELL-ADHESION; ACTIN CYTOSKELETON; PROTEIN; ALPHA; PHOSPHOINOSITIDES; CYTOHESIN-1;

D O I：

10.1073/pnas.0908423107

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables during epithelial polarization. However, the mechanisms by which this complex functions are not well elucidated. In the present study, we found that activation of Arf6 is spatiotemporally regulated as a downstream signaling pathway of the Par protein complex. When primordial AJs are formed, Par-3 recruits a scaffolding protein, termed the FERM domain containing 4A (FRMD4A). FRMD4A connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. We propose that the Par-3/FRMD4A/cytohesin-1 complex ensures accurate activation of Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization.

引用

页码：748 / 753

页数：6

共 39 条

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