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Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled
The proto-oncogenic kinase Abelson (Abl) regulates actin in response to cell signaling. Drosophila Abl is required in the nervous system, and also in epithelial cells, where it regulates adherens junction stability and actin organization. Abl acts at least in part via the actin regulator Enabled (En...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173720/ https://www.ncbi.nlm.nih.gov/pubmed/14676307 http://dx.doi.org/10.1083/jcb.200307026 |
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author | Grevengoed, Elizabeth E. Fox, Donald T. Gates, Julie Peifer, Mark |
author_facet | Grevengoed, Elizabeth E. Fox, Donald T. Gates, Julie Peifer, Mark |
author_sort | Grevengoed, Elizabeth E. |
collection | PubMed |
description | The proto-oncogenic kinase Abelson (Abl) regulates actin in response to cell signaling. Drosophila Abl is required in the nervous system, and also in epithelial cells, where it regulates adherens junction stability and actin organization. Abl acts at least in part via the actin regulator Enabled (Ena), but the mechanism by which Abl regulates Ena is unknown. We describe a novel role for Abl in early Drosophila development, where it regulates the site and type of actin structures produced. In Abl's absence, excess actin is polymerized in apical microvilli, whereas too little actin is assembled into pseudocleavage and cellularization furrows. These effects involve Ena misregulation. In abl mutants, Ena accumulates ectopically at the apical cortex where excess actin is observed, suggesting that Abl regulates Ena's subcellular localization. We also examined other actin regulators. Loss of Abl leads to changes in the localization of the Arp2/3 complex and the formin Diaphanous, and mutations in diaphanous or capping protein β enhance abl phenotypes. |
format | Text |
id | pubmed-2173720 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21737202008-05-01 Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled Grevengoed, Elizabeth E. Fox, Donald T. Gates, Julie Peifer, Mark J Cell Biol Article The proto-oncogenic kinase Abelson (Abl) regulates actin in response to cell signaling. Drosophila Abl is required in the nervous system, and also in epithelial cells, where it regulates adherens junction stability and actin organization. Abl acts at least in part via the actin regulator Enabled (Ena), but the mechanism by which Abl regulates Ena is unknown. We describe a novel role for Abl in early Drosophila development, where it regulates the site and type of actin structures produced. In Abl's absence, excess actin is polymerized in apical microvilli, whereas too little actin is assembled into pseudocleavage and cellularization furrows. These effects involve Ena misregulation. In abl mutants, Ena accumulates ectopically at the apical cortex where excess actin is observed, suggesting that Abl regulates Ena's subcellular localization. We also examined other actin regulators. Loss of Abl leads to changes in the localization of the Arp2/3 complex and the formin Diaphanous, and mutations in diaphanous or capping protein β enhance abl phenotypes. The Rockefeller University Press 2003-12-22 /pmc/articles/PMC2173720/ /pubmed/14676307 http://dx.doi.org/10.1083/jcb.200307026 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 Grevengoed, Elizabeth E. Fox, Donald T. Gates, Julie Peifer, Mark Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled |
title | Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled |
title_full | Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled |
title_fullStr | Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled |
title_full_unstemmed | Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled |
title_short | Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled |
title_sort | balancing different types of actin polymerization at distinct sites: roles for abelson kinase and enabled |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173720/ https://www.ncbi.nlm.nih.gov/pubmed/14676307 http://dx.doi.org/10.1083/jcb.200307026 |
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