Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/344760
Type: Artigo
Title: alpha B-crystallin interacts with and prevents stress-activated proteolysis of focal adhesion kinase by calpain in cardiomyocytes
Author: Pereira, M. B. M.
Santos, A. M.
Goncalves, D. C.
Cardoso, A. C.
Consonni, S. R.
Gozzo, F. C.
Oliveira, P. S.
Pereira, A. H. M.
Figueiredo, A. R.
Tiroli-Cepeda, A. O.
Ramos, C. H. I.
Thomaz, A. A. de
Cesar, C. L.
Franchini, K. G.
Abstract: Focal adhesion kinase (FAK) contributes to cellular homeostasis under stress conditions. Here we show that alpha B-crystallin interacts with and confers protection to FAK against calpain-mediated proteolysis in cardiomyocytes. A hydrophobic patch mapped between helices 1 and 4 of the FAK FAT domain was found to bind to the beta 4-beta 8 groove of alpha B-crystallin. Such an interaction requires FAK tyrosine 925 and is enhanced following its phosphorylation by Src, which occurs upon FAK stimulation. alpha B-crystallin silencing results in calpain-dependent FAK depletion and in the increased apoptosis of cardiomyocytes in response to mechanical stress. FAK overexpression protects cardiomyocytes depleted of alpha B-crystallin against the stretch-induced apoptosis. Consistently, load-induced apoptosis is blunted in the hearts from cardiac-specific FAK transgenic mice transiently depleted of alpha B-crystallin by RNA interference. These studies define a role for alpha B-crystallin in controlling FAK function and cardiomyocyte survival through the prevention of calpain-mediated degradation of FAK.
Subject: Tumores
Experimentação animal
Apoptose
Adesão
Country: Reino Unido
Editor: Nature Publishing Group
Rights: aberto
Identifier DOI: 10.1038/ncomms6159
Address: https://www.nature.com/articles/ncomms6159
Date Issue: 2014
Appears in Collections:IQ - Artigos e Outros Documentos
IFGW - Artigos e Outros Documentos
FCM - Artigos e Outros Documentos

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