Interplay of MPP5a with Rab11 synergistically builds epithelial apical polarity and zonula adherens. Development 2020 Nov 19;147(22)
Date
10/17/2020Pubmed ID
33060129DOI
10.1242/dev.184457Scopus ID
2-s2.0-85096508420 (requires institutional sign-in at Scopus site) 1 CitationAbstract
Adherens junction remodeling regulated by apical polarity proteins constitutes a major driving force for tissue morphogenesis, although the precise mechanism remains inconclusive. Here, we report that, in zebrafish, the Crumbs complex component MPP5a interacts with small GTPase Rab11 in Golgi to transport cadherin and Crumbs components synergistically to the apical domain, thus establishing apical epithelial polarity and adherens junctions. In contrast, Par complex recruited by MPP5a is incapable of interacting with Rab11 but might assemble cytoskeleton to facilitate cadherin exocytosis. In accordance, dysfunction of MPP5a induces an invasive migration of epithelial cells. This adherens junction remodeling pattern is frequently observed in zebrafish lens epithelial cells and neuroepithelial cells. The data identify an unrecognized MPP5a-Rab11 complex and describe its essential role in guiding apical polarization and zonula adherens formation in epithelial cells.
Author List
Hao Y, Zhou Y, Yu Y, Zheng M, Weng K, Kou Z, Liang J, Zhang Q, Tang X, Xu P, Link BA, Yao K, Zou JAuthor
Brian A. Link PhD Professor in the Cell Biology, Neurobiology and Anatomy department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adherens JunctionsAnimals
Cadherins
Cell Movement
Cell Polarity
Epithelial Cells
Golgi Apparatus
Guanylate Cyclase
Protein Transport
Zebrafish
Zebrafish Proteins
rab GTP-Binding Proteins
