Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 2, Pages 748-753Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0908423107
Keywords
adherens junction; tight junction; cell polarity; epithelial cells; cytohesin
Categories
Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency
- Biotechnology and Biological Sciences Research Council [P20180] Funding Source: researchfish
- Grants-in-Aid for Scientific Research [21687016, 22390014] Funding Source: KAKEN
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
