FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex.
basic_science · Level V
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- Record sourced from PubMed, PMID 20080746.
- Also identified by DOI 10.1073/pnas.0908423107 and PMC identifier 2818900.
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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.
Medical subject headings
- Adherens Junctions
- Epithelial Cells