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Novel role of cPLA(2)α in membrane and actin dynamics

Actin-directed processes such as membrane ruffling and cell migration are regulated by specific signal transduction pathways that become activated by growth factor receptors. The same signaling pathways that lead to modifications in actin dynamics also activate cPLA(2)α. Moreover, arachidonic acid,...

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Detalles Bibliográficos
Autores principales: Moes, Maarten, Boonstra, Johannes, Regan-Klapisz, Elsa
Formato: Texto
Lenguaje:English
Publicado: SP Birkhäuser Verlag Basel 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856858/
https://www.ncbi.nlm.nih.gov/pubmed/20112044
http://dx.doi.org/10.1007/s00018-010-0267-0
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author Moes, Maarten
Boonstra, Johannes
Regan-Klapisz, Elsa
author_facet Moes, Maarten
Boonstra, Johannes
Regan-Klapisz, Elsa
author_sort Moes, Maarten
collection PubMed
description Actin-directed processes such as membrane ruffling and cell migration are regulated by specific signal transduction pathways that become activated by growth factor receptors. The same signaling pathways that lead to modifications in actin dynamics also activate cPLA(2)α. Moreover, arachidonic acid, the product of cPLA(2)α activity, is involved in regulation of actin dynamics. Therefore, it was investigated whether cPLA(2)α plays a role in actin dynamics, more specifically during growth factor-induced membrane ruffling and cell migration. Upon stimulation of ruffling and cell migration by growth factors, endogenous cPLA(2)α and its active phosphorylated form were shown to relocate at protrusions of the cell membrane involved in actin and membrane dynamics. Inhibition of cPLA(2)α activity with specific inhibitors blocked growth factor-induced membrane and actin dynamics, suggesting an important role for cPLA(2)α in these processes.
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spelling pubmed-28568582010-04-27 Novel role of cPLA(2)α in membrane and actin dynamics Moes, Maarten Boonstra, Johannes Regan-Klapisz, Elsa Cell Mol Life Sci Research Article Actin-directed processes such as membrane ruffling and cell migration are regulated by specific signal transduction pathways that become activated by growth factor receptors. The same signaling pathways that lead to modifications in actin dynamics also activate cPLA(2)α. Moreover, arachidonic acid, the product of cPLA(2)α activity, is involved in regulation of actin dynamics. Therefore, it was investigated whether cPLA(2)α plays a role in actin dynamics, more specifically during growth factor-induced membrane ruffling and cell migration. Upon stimulation of ruffling and cell migration by growth factors, endogenous cPLA(2)α and its active phosphorylated form were shown to relocate at protrusions of the cell membrane involved in actin and membrane dynamics. Inhibition of cPLA(2)α activity with specific inhibitors blocked growth factor-induced membrane and actin dynamics, suggesting an important role for cPLA(2)α in these processes. SP Birkhäuser Verlag Basel 2010-01-29 2010 /pmc/articles/PMC2856858/ /pubmed/20112044 http://dx.doi.org/10.1007/s00018-010-0267-0 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Research Article
Moes, Maarten
Boonstra, Johannes
Regan-Klapisz, Elsa
Novel role of cPLA(2)α in membrane and actin dynamics
title Novel role of cPLA(2)α in membrane and actin dynamics
title_full Novel role of cPLA(2)α in membrane and actin dynamics
title_fullStr Novel role of cPLA(2)α in membrane and actin dynamics
title_full_unstemmed Novel role of cPLA(2)α in membrane and actin dynamics
title_short Novel role of cPLA(2)α in membrane and actin dynamics
title_sort novel role of cpla(2)α in membrane and actin dynamics
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856858/
https://www.ncbi.nlm.nih.gov/pubmed/20112044
http://dx.doi.org/10.1007/s00018-010-0267-0
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