p38alpha MAPK can positively or negatively regulate Rac-1 activity depending on the presence of serum

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dc.contributor.authorZuluaga, Susana
dc.contributor.authorGutiérrez Uzquiza, Álvaro
dc.contributor.authorBragado, Paloma
dc.contributor.authorAlvarez-Barrientos, Alberto
dc.contributor.authorBenito De Las Heras, Manuel R.
dc.contributor.authorNebreda, Angel R
dc.contributor.authorPorras Gallo, María Almudena
dc.date.accessioned2024-01-12T09:47:22Z
dc.date.available2024-01-12T09:47:22Z
dc.date.issued2007
dc.description.abstractThe small GTP-ase Rac-1 can trigger p38 MAPK activation and, in turn, p38alpha can regulate signalling pathways that potentially impinge on Rac-1 activity. We have investigated the cross-talk between p38alpha and Rac-1 and found that p38alpha regulates the association between Rac-1 and caveolin-1 in serum-deprived cardiomyocytes. This interaction depends on cell attachment and correlates with higher levels of active Rac-1. Actin organization might regulate the formation of Rac-1-caveolin-1 complexes. In contrast, the Rac-1-caveolin-1 interaction is almost undetectable in the presence of serum, where Rac-1 activity is negatively regulated by p38alpha. Our results indicate that p38alpha can differentially contribute to Rac-1 activation depending on the presence of serum.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Farmacia
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Sanidad (España)
dc.description.sponsorshipMinisterio de Educación y Ciencia (España)
dc.description.sponsorshipComunidad de Madrid
dc.description.statuspub
dc.identifier.citationFraguas-Sánchez AI, Fernández-Carballido A, Martin-Sabroso C, Torres-Suárez AI. Stability characteristics of cannabidiol for the design of pharmacological, biochemical and pharmaceutical studies. Journal of Chromatography B 2020;1150:122188. https://doi.org/10.1016/j.jchromb.2020.122188.
dc.identifier.doi10.1016/j.febslet.2007.06.078
dc.identifier.essn1873-3468
dc.identifier.issn0014-5793
dc.identifier.officialurlhttps://doi.org/10.1016/j.febslet.2007.06.078
dc.identifier.relatedurlhttps://febs.onlinelibrary.wiley.com/doi/10.1016/j.febslet.2007.06.078
dc.identifier.urihttps://hdl.handle.net/20.500.14352/92697
dc.issue.number20
dc.journal.titleFEBS Letters
dc.language.isoeng
dc.page.final3825
dc.page.initial3819
dc.relation.projectIDinfo:eu-repo/grantAgreement/PI041131
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.accessRightsrestricted access
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.cdu665
dc.subject.keywordp38 MAPK
dc.subject.keywordCardiomyocyte
dc.subject.keywordActin
dc.subject.keywordAdhesion
dc.subject.keywordCaveolin-1
dc.subject.keywordRac-1
dc.subject.ucmBioquímica (Farmacia)
dc.subject.unesco23 Química
dc.titlep38alpha MAPK can positively or negatively regulate Rac-1 activity depending on the presence of serum
dc.typejournal article
dc.volume.number581
dspace.entity.typePublication
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relation.isAuthorOfPublication6a240551-5797-4599-8d91-76bc38fecf8d
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relation.isAuthorOfPublication.latestForDiscoveryfe7d7e09-f48f-4104-b627-5f056790b029
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