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Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells

Cellular levels of p120 catenin function as a set point for cadherin expression levels in... The mechanisms by which catenins regulate cadherin function are not fully understood, and the precise function of p120 catenin (p120ctn) has remained particularly elusive. In microvascular endothelial cells, p120ctn colocalized extensively with cell surface VE-cadherin, but failed to colocalize with VE-cadherin that had entered intracellular degradative compartments. To test the possibility that p120ctn binding to VE-cadherin regulates VE-cadherin internalization, a series of approaches were undertaken to manipulate p120ctn availability to endogenous VE-cadherin. Expression of VE-cadherin mutants that competed for p120ctn binding triggered the degradation of endogenous VE-cadherin. Similarly, reducing levels of p120ctn using siRNA caused a dramatic and dose-related reduction in cellular levels of VE-cadherin. In contrast, overexpression of p120ctn increased VE-cadherin cell surface levels and inhibited entry of cell surface VE-cadherin into degradative compartments. These results demonstrate that cellular levels of p120ctn function as a set point mechanism that regulates cadherin expression levels, and that a major function of p120ctn is to control cadherin internalization and degradation. adhesion; cytoskeleton; endocytosis; cadherin; catenin Footnotes Abbreviations used in this paper: IL-2R, interleukin-2 receptor; MEC, microvascular endothelial cells; p120ctn, p120 catenin. Submitted: 2 June 2003 Accepted: 19 September 2003 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells

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Publisher
Rockefeller University Press
Copyright
© 2003 Rockefeller University Press
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.200306001
pmid
14610056
Publisher site
See Article on Publisher Site

Abstract

The mechanisms by which catenins regulate cadherin function are not fully understood, and the precise function of p120 catenin (p120ctn) has remained particularly elusive. In microvascular endothelial cells, p120ctn colocalized extensively with cell surface VE-cadherin, but failed to colocalize with VE-cadherin that had entered intracellular degradative compartments. To test the possibility that p120ctn binding to VE-cadherin regulates VE-cadherin internalization, a series of approaches were undertaken to manipulate p120ctn availability to endogenous VE-cadherin. Expression of VE-cadherin mutants that competed for p120ctn binding triggered the degradation of endogenous VE-cadherin. Similarly, reducing levels of p120ctn using siRNA caused a dramatic and dose-related reduction in cellular levels of VE-cadherin. In contrast, overexpression of p120ctn increased VE-cadherin cell surface levels and inhibited entry of cell surface VE-cadherin into degradative compartments. These results demonstrate that cellular levels of p120ctn function as a set point mechanism that regulates cadherin expression levels, and that a major function of p120ctn is to control cadherin internalization and degradation. adhesion; cytoskeleton; endocytosis; cadherin; catenin Footnotes Abbreviations used in this paper: IL-2R, interleukin-2 receptor; MEC, microvascular endothelial cells; p120ctn, p120 catenin. Submitted: 2 June 2003 Accepted: 19 September 2003

Journal

The Journal of Cell BiologyRockefeller University Press

Published: Nov 10, 2003

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