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

Junichi Ikenouchi, Masato Umeda

研究成果: ジャーナルへの寄稿記事

44 引用 (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.

元の言語英語
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
発行部数2
DOI
出版物ステータス出版済み - 2 15 2010
外部発表Yes

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Adherens Junctions
Guanine Nucleotide Exchange Factors
Actin Cytoskeleton
Actins
Proteins
Membranes
cytohesin-1

All Science Journal Classification (ASJC) codes

  • General

これを引用

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abstract = "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.",
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