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

Junichi Ikenouchi, Masato Umeda

研究成果: Contribution to journalArticle査読

49 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)748-753
ページ数6
ジャーナルProceedings of the National Academy of Sciences of the United States of America
107
2
DOI
出版ステータス出版済み - 2010

All Science Journal Classification (ASJC) codes

  • General

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