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RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation

Adipocyte differentiation can be regulated by the combined activity of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). In particular, PTPs act as key regulators in differentiation-associated signaling pathways. We recently found that receptor-type PTPμ (RPTPμ) expression is...

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Autores principales: Kim, Won Kon, Jung, Hyeyun, Kim, Eun Young, Kim, Do Hyung, Cho, Yee Sook, Park, Byoung Chul, Park, Sung Goo, Ko, Yong, Bae, Kwang-Hee, Lee, Sang Chul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237630/
https://www.ncbi.nlm.nih.gov/pubmed/21998202
http://dx.doi.org/10.1091/mbc.E11-03-0175
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author Kim, Won Kon
Jung, Hyeyun
Kim, Eun Young
Kim, Do Hyung
Cho, Yee Sook
Park, Byoung Chul
Park, Sung Goo
Ko, Yong
Bae, Kwang-Hee
Lee, Sang Chul
author_facet Kim, Won Kon
Jung, Hyeyun
Kim, Eun Young
Kim, Do Hyung
Cho, Yee Sook
Park, Byoung Chul
Park, Sung Goo
Ko, Yong
Bae, Kwang-Hee
Lee, Sang Chul
author_sort Kim, Won Kon
collection PubMed
description Adipocyte differentiation can be regulated by the combined activity of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). In particular, PTPs act as key regulators in differentiation-associated signaling pathways. We recently found that receptor-type PTPμ (RPTPμ) expression is markedly increased during the adipogenic differentiation of 3T3-L1 preadipocytes and mesenchymal stem cells. Here, we investigate the functional roles of RPTPμ and the mechanism of its involvement in the regulation of signal transduction during adipogenesis of 3T3-L1 cells. Depletion of endogenous RPTPμ by RNA interference significantly inhibited adipogenic differentiation, whereas RPTPμ overexpression led to an increase in adipogenic differentiation. Ectopic expression of p120 catenin suppressed adipocyte differentiation, and the decrease in adipogenesis by p120 catenin was recovered by introducing RPTPμ. Moreover, RPTPμ induced a decrease in the cytoplasmic p120 catenin expression by reducing its tyrosine phosphorylation level, consequently leading to enhanced translocation of Glut-4 to the plasma membrane. On the basis of these results, we propose that RPTPμ acts as a positive regulator of adipogenesis by modulating the cytoplasmic p120 catenin level. Our data conclusively demonstrate that differentiation into adipocytes is controlled by RPTPμ, supporting the utility of RPTPμ and p120 catenin as novel target proteins for the treatment of obesity.
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spelling pubmed-32376302012-03-01 RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation Kim, Won Kon Jung, Hyeyun Kim, Eun Young Kim, Do Hyung Cho, Yee Sook Park, Byoung Chul Park, Sung Goo Ko, Yong Bae, Kwang-Hee Lee, Sang Chul Mol Biol Cell Articles Adipocyte differentiation can be regulated by the combined activity of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). In particular, PTPs act as key regulators in differentiation-associated signaling pathways. We recently found that receptor-type PTPμ (RPTPμ) expression is markedly increased during the adipogenic differentiation of 3T3-L1 preadipocytes and mesenchymal stem cells. Here, we investigate the functional roles of RPTPμ and the mechanism of its involvement in the regulation of signal transduction during adipogenesis of 3T3-L1 cells. Depletion of endogenous RPTPμ by RNA interference significantly inhibited adipogenic differentiation, whereas RPTPμ overexpression led to an increase in adipogenic differentiation. Ectopic expression of p120 catenin suppressed adipocyte differentiation, and the decrease in adipogenesis by p120 catenin was recovered by introducing RPTPμ. Moreover, RPTPμ induced a decrease in the cytoplasmic p120 catenin expression by reducing its tyrosine phosphorylation level, consequently leading to enhanced translocation of Glut-4 to the plasma membrane. On the basis of these results, we propose that RPTPμ acts as a positive regulator of adipogenesis by modulating the cytoplasmic p120 catenin level. Our data conclusively demonstrate that differentiation into adipocytes is controlled by RPTPμ, supporting the utility of RPTPμ and p120 catenin as novel target proteins for the treatment of obesity. The American Society for Cell Biology 2011-12-15 /pmc/articles/PMC3237630/ /pubmed/21998202 http://dx.doi.org/10.1091/mbc.E11-03-0175 Text en © 2011 Kim et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Kim, Won Kon
Jung, Hyeyun
Kim, Eun Young
Kim, Do Hyung
Cho, Yee Sook
Park, Byoung Chul
Park, Sung Goo
Ko, Yong
Bae, Kwang-Hee
Lee, Sang Chul
RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
title RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
title_full RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
title_fullStr RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
title_full_unstemmed RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
title_short RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
title_sort rptpμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237630/
https://www.ncbi.nlm.nih.gov/pubmed/21998202
http://dx.doi.org/10.1091/mbc.E11-03-0175
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