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Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component
Cadherin–catenin complexes, localized to adherens junctions, are essential for cell–cell adhesion. One means of regulating adhesion is through the juxtamembrane domain of the cadherin cytoplasmic tail. This region is the binding site for p120, leading to the hypothesis that p120 is a key regulator o...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172674/ https://www.ncbi.nlm.nih.gov/pubmed/12551951 http://dx.doi.org/10.1083/jcb.200211083 |
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author | Myster, Steven H. Cavallo, Robert Anderson, Charles T. Fox, Donald T. Peifer, Mark |
author_facet | Myster, Steven H. Cavallo, Robert Anderson, Charles T. Fox, Donald T. Peifer, Mark |
author_sort | Myster, Steven H. |
collection | PubMed |
description | Cadherin–catenin complexes, localized to adherens junctions, are essential for cell–cell adhesion. One means of regulating adhesion is through the juxtamembrane domain of the cadherin cytoplasmic tail. This region is the binding site for p120, leading to the hypothesis that p120 is a key regulator of cell adhesion. p120 has also been suggested to regulate the GTPase Rho and to regulate transcription via its binding partner Kaiso. To test these hypothesized functions, we turned to Drosophila, which has only a single p120 family member. It localizes to adherens junctions and binds the juxtamembrane region of DE-cadherin (DE-cad). We generated null alleles of p120 and found that mutants are viable and fertile and have no substantial changes in junction structure or function. However, p120 mutations strongly enhance mutations in the genes encoding DE-cadherin or Armadillo, the β-catenin homologue. Finally, we examined the localization of p120 during embryogenesis. p120 localizes to adherens junctions, but its localization there is less universal than that of core adherens junction proteins. Together, these data suggest that p120 is an important positive modulator of adhesion but that it is not an essential core component of adherens junctions. |
format | Text |
id | pubmed-2172674 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21726742008-05-01 Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component Myster, Steven H. Cavallo, Robert Anderson, Charles T. Fox, Donald T. Peifer, Mark J Cell Biol Article Cadherin–catenin complexes, localized to adherens junctions, are essential for cell–cell adhesion. One means of regulating adhesion is through the juxtamembrane domain of the cadherin cytoplasmic tail. This region is the binding site for p120, leading to the hypothesis that p120 is a key regulator of cell adhesion. p120 has also been suggested to regulate the GTPase Rho and to regulate transcription via its binding partner Kaiso. To test these hypothesized functions, we turned to Drosophila, which has only a single p120 family member. It localizes to adherens junctions and binds the juxtamembrane region of DE-cadherin (DE-cad). We generated null alleles of p120 and found that mutants are viable and fertile and have no substantial changes in junction structure or function. However, p120 mutations strongly enhance mutations in the genes encoding DE-cadherin or Armadillo, the β-catenin homologue. Finally, we examined the localization of p120 during embryogenesis. p120 localizes to adherens junctions, but its localization there is less universal than that of core adherens junction proteins. Together, these data suggest that p120 is an important positive modulator of adhesion but that it is not an essential core component of adherens junctions. The Rockefeller University Press 2003-02-03 /pmc/articles/PMC2172674/ /pubmed/12551951 http://dx.doi.org/10.1083/jcb.200211083 Text en Copyright © 2003, The Rockefeller University Press 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 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Myster, Steven H. Cavallo, Robert Anderson, Charles T. Fox, Donald T. Peifer, Mark Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
title |
Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
title_full |
Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
title_fullStr |
Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
title_full_unstemmed |
Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
title_short |
Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
title_sort | drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172674/ https://www.ncbi.nlm.nih.gov/pubmed/12551951 http://dx.doi.org/10.1083/jcb.200211083 |
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