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Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart
The GTPase Cdc42 was among the original genes identified with roles in cell polarity, and interest in its cellular roles from yeast to humans remains high. Cdc42 is a well-known regulator of the actin cytoskeleton, but also plays important roles in vesicular trafficking. In this issue, Harris and Te...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2600754/ https://www.ncbi.nlm.nih.gov/pubmed/19064672 http://dx.doi.org/10.1083/jcb.200811057 |
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author | Duncan, Mara C. Peifer, Mark |
author_facet | Duncan, Mara C. Peifer, Mark |
author_sort | Duncan, Mara C. |
collection | PubMed |
description | The GTPase Cdc42 was among the original genes identified with roles in cell polarity, and interest in its cellular roles from yeast to humans remains high. Cdc42 is a well-known regulator of the actin cytoskeleton, but also plays important roles in vesicular trafficking. In this issue, Harris and Tepass (Harris, K.P, and U. Tepass. 2008. J. Cell. Biol. 183:1129–1143) provide new insights into how Cdc42 and Par proteins work together to modulate cell adhesion and polarity during embryonic morphogenesis by regulating the traffic of key cell junction proteins. |
format | Text |
id | pubmed-2600754 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-26007542009-06-15 Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart Duncan, Mara C. Peifer, Mark J Cell Biol Reviews The GTPase Cdc42 was among the original genes identified with roles in cell polarity, and interest in its cellular roles from yeast to humans remains high. Cdc42 is a well-known regulator of the actin cytoskeleton, but also plays important roles in vesicular trafficking. In this issue, Harris and Tepass (Harris, K.P, and U. Tepass. 2008. J. Cell. Biol. 183:1129–1143) provide new insights into how Cdc42 and Par proteins work together to modulate cell adhesion and polarity during embryonic morphogenesis by regulating the traffic of key cell junction proteins. The Rockefeller University Press 2008-12-15 /pmc/articles/PMC2600754/ /pubmed/19064672 http://dx.doi.org/10.1083/jcb.200811057 Text en © 2008 Duncan and Peifer 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.jcb.org/misc/terms.shtml). 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 Duncan, Mara C. Peifer, Mark Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart |
title | Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart |
title_full | Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart |
title_fullStr | Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart |
title_full_unstemmed | Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart |
title_short | Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart |
title_sort | regulating polarity by directing traffic: cdc42 prevents adherens junctions from crumblin' apart |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2600754/ https://www.ncbi.nlm.nih.gov/pubmed/19064672 http://dx.doi.org/10.1083/jcb.200811057 |
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