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α-Catenin phosphorylation promotes intercellular adhesion through a dual-kinase mechanism
Journal article   Open access   Peer reviewed

α-Catenin phosphorylation promotes intercellular adhesion through a dual-kinase mechanism

David J Escobar, Ridhdhi Desai, Noboru Ishiyama, Stephen S Folmsbee, Megan N Novak, Annette S Flozak, Rebecca L Daugherty, Rigen Mo, Dhaval Nanavati, Ritu Sarpal, …
Journal of cell science, v 128(6), pp 1150-1165
15 Mar 2015
DOI: https://doi.org/10.1242/jcs.163824
PMID: 25653389
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://europepmc.org/articles/pmc4359922View
Published, Version of Record (VoR)Open Access (License Unspecified),  Open
url
https://doi.org/10.1242/jcs.163824View
Published, Version of Record (VoR) Open

Abstract

Actins - metabolism alpha Catenin - chemistry alpha Catenin - genetics alpha Catenin - metabolism Amino Acid Sequence Animals Apoptosis Blotting, Western Cadherins - genetics Cadherins - metabolism Casein Kinase I - genetics Casein Kinase I - metabolism Casein Kinase II - genetics Casein Kinase II - metabolism Cell Adhesion Cell Membrane - metabolism Cell Movement Cell Proliferation Cells, Cultured Colonic Neoplasms - metabolism Colonic Neoplasms - pathology Dogs Drosophila melanogaster - genetics Drosophila melanogaster - growth & development Drosophila melanogaster - metabolism Female Fluorescent Antibody Technique Humans Immunoprecipitation Madin Darby Canine Kidney Cells Molecular Sequence Data Ovary - cytology Ovary - metabolism Phosphorylation Protein Structure, Tertiary Sequence Homology, Amino Acid
The cadherin-catenin adhesion complex is a key contributor to epithelial tissue stability and dynamic cell movements during development and tissue renewal. How this complex is regulated to accomplish these functions is not fully understood. We identified several phosphorylation sites in mammalian αE-catenin (also known as catenin α-1) and Drosophila α-Catenin within a flexible linker located between the middle (M)-region and the carboxy-terminal actin-binding domain. We show that this phospho-linker (P-linker) is the main phosphorylated region of α-catenin in cells and is sequentially modified at casein kinase 2 and 1 consensus sites. In Drosophila, the P-linker is required for normal α-catenin function during development and collective cell migration, although no obvious defects were found in cadherin-catenin complex assembly or adherens junction formation. In mammalian cells, non-phosphorylatable forms of α-catenin showed defects in intercellular adhesion using a mechanical dispersion assay. Epithelial sheets expressing phosphomimetic forms of α-catenin showed faster and more coordinated migrations after scratch wounding. These findings suggest that phosphorylation and dephosphorylation of the α-catenin P-linker are required for normal cadherin-catenin complex function in Drosophila and mammalian cells.

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Web of Science research areas
Cell Biology
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