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

Junichi Ikenouchi, Masato Umeda

Research output: Contribution to journalArticlepeer-review

69 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)748-753
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number2
Publication statusPublished - 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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