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Guilt by association: What p120-catenin has to hide
Members of the p120-catenin family associate with cadherins and regulate their stability at the plasma membrane. How p120-catenin limits cadherin endocytosis has long remained a mystery. In this issue, Nanes et al. (2012. J. Cell Biol. doi:10.1083/jcb.201205029) identify a conserved acidic motif wit...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3471234/ https://www.ncbi.nlm.nih.gov/pubmed/23071151 http://dx.doi.org/10.1083/jcb.201209014 |
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author | Perez-Moreno, Mirna Fuchs, Elaine |
author_facet | Perez-Moreno, Mirna Fuchs, Elaine |
author_sort | Perez-Moreno, Mirna |
collection | PubMed |
description | Members of the p120-catenin family associate with cadherins and regulate their stability at the plasma membrane. How p120-catenin limits cadherin endocytosis has long remained a mystery. In this issue, Nanes et al. (2012. J. Cell Biol. doi:10.1083/jcb.201205029) identify a conserved acidic motif within cadherins that acts as a physical platform for p120-catenin binding. However, in the absence of p120-catenin, the motif acts as an endocytic signal. These results provide new insight into p120-catenin’s role as guardian of intercellular junction dynamics. |
format | Online Article Text |
id | pubmed-3471234 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-34712342013-04-15 Guilt by association: What p120-catenin has to hide Perez-Moreno, Mirna Fuchs, Elaine J Cell Biol Reviews Members of the p120-catenin family associate with cadherins and regulate their stability at the plasma membrane. How p120-catenin limits cadherin endocytosis has long remained a mystery. In this issue, Nanes et al. (2012. J. Cell Biol. doi:10.1083/jcb.201205029) identify a conserved acidic motif within cadherins that acts as a physical platform for p120-catenin binding. However, in the absence of p120-catenin, the motif acts as an endocytic signal. These results provide new insight into p120-catenin’s role as guardian of intercellular junction dynamics. The Rockefeller University Press 2012-10-15 /pmc/articles/PMC3471234/ /pubmed/23071151 http://dx.doi.org/10.1083/jcb.201209014 Text en © 2012 Perez-Moreno and Fuchs This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Reviews Perez-Moreno, Mirna Fuchs, Elaine Guilt by association: What p120-catenin has to hide |
title | Guilt by association: What p120-catenin has to hide |
title_full | Guilt by association: What p120-catenin has to hide |
title_fullStr | Guilt by association: What p120-catenin has to hide |
title_full_unstemmed | Guilt by association: What p120-catenin has to hide |
title_short | Guilt by association: What p120-catenin has to hide |
title_sort | guilt by association: what p120-catenin has to hide |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3471234/ https://www.ncbi.nlm.nih.gov/pubmed/23071151 http://dx.doi.org/10.1083/jcb.201209014 |
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