Cargando…

Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling

The ILK, PINCH, Parvin (IPP) complex regulates adhesion and migration via binding of ILK to β1 integrin and α−parvin thus linking focal adhesions to actin cytoskeleton. ILK also binds the adaptor protein PINCH which connects signaling proteins including Rsu1 to the complex. A recent study of Rsu1 an...

Descripción completa

Detalles Bibliográficos
Autores principales: Kim, Yong-Chul, Gonzalez-Nieves, Reyda, Cutler, Mary L
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4594256/
https://www.ncbi.nlm.nih.gov/pubmed/25482629
http://dx.doi.org/10.4161/19336918.2014.972775
_version_ 1782393427860652032
author Kim, Yong-Chul
Gonzalez-Nieves, Reyda
Cutler, Mary L
author_facet Kim, Yong-Chul
Gonzalez-Nieves, Reyda
Cutler, Mary L
author_sort Kim, Yong-Chul
collection PubMed
description The ILK, PINCH, Parvin (IPP) complex regulates adhesion and migration via binding of ILK to β1 integrin and α−parvin thus linking focal adhesions to actin cytoskeleton. ILK also binds the adaptor protein PINCH which connects signaling proteins including Rsu1 to the complex. A recent study of Rsu1 and PINCH1 in non-transformed MCF10A human mammary epithelial cells revealed that the siRNA-mediated depletion of either Rsu1 or PINCH1 decreased the number of focal adhesions (FAs) and altered the distribution and localization of FA proteins. This correlated with reduced adhesion, failure to spread or migrate in response to EGF and a loss of actin stress fibers and caveolae. The depletion of Rsu1 caused significant reduction in PINCH1 implying that Rsu1 may function in part by regulating levels of PINCH1. However, Rsu1, but not PINCH1, was required for EGF-induced activation of p38 Map kinase and ATF2 phosphorylation, suggesting a Rsu1 function independent from the IPP complex. Reconstitution of Rsu1-depleted cells with a Rsu1 mutant (N92D) that does not bind to PINCH1 failed to restore FAs or migration but did promote IPP-independent spreading and constitutive as well as EGF-induced p38 activation. In this commentary we discuss p38 activity in adhesion and how Rsu1 expression may be linked to Map kinase kinase (MKK) activation and detachment-induced stress kinase signaling.
format Online
Article
Text
id pubmed-4594256
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Taylor & Francis
record_format MEDLINE/PubMed
spelling pubmed-45942562015-10-23 Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling Kim, Yong-Chul Gonzalez-Nieves, Reyda Cutler, Mary L Cell Adh Migr Commentary The ILK, PINCH, Parvin (IPP) complex regulates adhesion and migration via binding of ILK to β1 integrin and α−parvin thus linking focal adhesions to actin cytoskeleton. ILK also binds the adaptor protein PINCH which connects signaling proteins including Rsu1 to the complex. A recent study of Rsu1 and PINCH1 in non-transformed MCF10A human mammary epithelial cells revealed that the siRNA-mediated depletion of either Rsu1 or PINCH1 decreased the number of focal adhesions (FAs) and altered the distribution and localization of FA proteins. This correlated with reduced adhesion, failure to spread or migrate in response to EGF and a loss of actin stress fibers and caveolae. The depletion of Rsu1 caused significant reduction in PINCH1 implying that Rsu1 may function in part by regulating levels of PINCH1. However, Rsu1, but not PINCH1, was required for EGF-induced activation of p38 Map kinase and ATF2 phosphorylation, suggesting a Rsu1 function independent from the IPP complex. Reconstitution of Rsu1-depleted cells with a Rsu1 mutant (N92D) that does not bind to PINCH1 failed to restore FAs or migration but did promote IPP-independent spreading and constitutive as well as EGF-induced p38 activation. In this commentary we discuss p38 activity in adhesion and how Rsu1 expression may be linked to Map kinase kinase (MKK) activation and detachment-induced stress kinase signaling. Taylor & Francis 2014-10-23 /pmc/articles/PMC4594256/ /pubmed/25482629 http://dx.doi.org/10.4161/19336918.2014.972775 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Commentary
Kim, Yong-Chul
Gonzalez-Nieves, Reyda
Cutler, Mary L
Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling
title Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling
title_full Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling
title_fullStr Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling
title_full_unstemmed Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling
title_short Rsu1 contributes to cell adhesion and spreading in MCF10A cells via effects on P38 map kinase signaling
title_sort rsu1 contributes to cell adhesion and spreading in mcf10a cells via effects on p38 map kinase signaling
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4594256/
https://www.ncbi.nlm.nih.gov/pubmed/25482629
http://dx.doi.org/10.4161/19336918.2014.972775
work_keys_str_mv AT kimyongchul rsu1contributestocelladhesionandspreadinginmcf10acellsviaeffectsonp38mapkinasesignaling
AT gonzaleznievesreyda rsu1contributestocelladhesionandspreadinginmcf10acellsviaeffectsonp38mapkinasesignaling
AT cutlermaryl rsu1contributestocelladhesionandspreadinginmcf10acellsviaeffectsonp38mapkinasesignaling