IMR Press / FBL / Volume 14 / Issue 6 / DOI: 10.2741/3366

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Rab family small G proteins in regulation of epithelial apical junctions
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1 Department of Biochemistry, Institute of Health Biosciences, The University of Tokushima Graduate School, 3-18-15 Kuramoto-cho, Tokushima 770-8503, Japan
Academic Editor:Andrei Ivanov
Front. Biosci. (Landmark Ed) 2009, 14(6), 2115–2129; https://doi.org/10.2741/3366
Published: 1 January 2009
(This article belongs to the Special Issue Molecular engines that build and break epithelial junctions)
Abstract

Tight junctions (TJs) and adherens junctions (AJs) comprise epithelial apical junctions that adhere neighboring epithelial cells and determine tissue organization. They are highly dynamic structures that undergo continuous remodeling during physiological morphogenesis and under pathological conditions. The assembly and disassembly of epithelial apical junctions is regulated by the interplay between a variety of cellular processes, such as the remodeling of actin cytoskeletons and the endocytic recycling of apical junctional proteins, and coordinated by many signaling pathways. Accumulating evidences demonstrate that Rab family small G proteins are crucially involved in the regulation of epithelial apical junctions. Rab proteins localized both at endosomes and apical junctions can influence the assembly and disassembly of epithelial apical junctions. In this review, we summarize how Rab proteins influence epithelial apical junctions and describe the role of Rab8/13-a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) complexes in the regulation of epithelial apical junctions.

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