p120-Catenin Inhibits VE-Cadherin Internalization through a Rho-independent Mechanism
| Autor: | Peter A. Vincent, Victor Faundez, Kristin B. Wittich, Christine M. Chiasson, Andrew P. Kowalczyk |
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| Rok vydání: | 2009 |
| Předmět: |
Dynamins
Male Delta Catenin animal structures media_common.quotation_subject Cell Adaptor Protein Complex 2 Biology Endocytosis Clathrin Membrane Microdomains Antigens CD medicine Humans Internalization Molecular Biology media_common Cell adhesion molecule Cadherin Endothelial Cells Catenins Articles Cell Biology Cadherins Phosphoproteins Cell biology medicine.anatomical_structure Catenin Mutation embryonic structures biology.protein VE-cadherin rhoA GTP-Binding Protein Cell Adhesion Molecules Protein Binding |
| Zdroj: | Molecular Biology of the Cell. 20:1970-1980 |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e08-07-0735 |
| Popis: | p120-catenin is a cytoplasmic binding partner of cadherins and functions as a set point for cadherin expression by preventing cadherin endocytosis, and degradation. p120 is known to regulate cell motility and invasiveness by inhibiting RhoA activity. However, the relationship between these functions of p120 is not understood. Here, we provide evidence that p120 functions as part of a plasma membrane retention mechanism for VE-cadherin by preventing the recruitment of VE-cadherin into membrane domains enriched in components of the endocytic machinery, including clathrin and the adaptor complex AP-2. The mechanism by which p120 regulates VE-cadherin entry into endocytic compartments is dependent on p120's interaction with the cadherin juxtamembrane domain, but occurs independently of p120's prevention of Rho GTPase activity. These findings clarify the mechanism for p120's function in stabilizing VE-cadherin at the plasma membrane and demonstrate a novel role for p120 in modulating the availability of cadherins for entry into a clathrin-dependent endocytic pathway. |
| Databáze: | OpenAIRE |
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