αB-crystallin interacts with and prevents stress-activated proteolysis of focal adhesion kinase by calpain in cardiomyocytes

Michelle B. M. Pereira, Aline M. Santos, Danieli C. Gonçalves, Alisson C. Cardoso, Sílvio R. Consonni, Fabio C. Gozzo, Paulo S. Oliveira, Ana Helena M. Pereira, Alana R. Figueiredo, Ana O. Tiroli-Cepeda, Carlos H. I. Ramos, André A. de Thomaz, Carlos L. Cesar and Kleber G. Franchini ()
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Michelle B. M. Pereira: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Aline M. Santos: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Danieli C. Gonçalves: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Alisson C. Cardoso: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Sílvio R. Consonni: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Fabio C. Gozzo: Chemistry Institute, University of Campinas
Paulo S. Oliveira: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Ana Helena M. Pereira: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials
Alana R. Figueiredo: Chemistry Institute, University of Campinas
Ana O. Tiroli-Cepeda: Chemistry Institute, University of Campinas
Carlos H. I. Ramos: Chemistry Institute, University of Campinas
André A. de Thomaz: Gleb Wataghin Physics Institute, University of Campinas
Carlos L. Cesar: Gleb Wataghin Physics Institute, University of Campinas
Kleber G. Franchini: Brazilian National Laboratory for Biosciences, Center for Research in Energy and Materials

Nature Communications, 2014, vol. 5, issue 1, 1-18

Abstract: Abstract Focal adhesion kinase (FAK) contributes to cellular homeostasis under stress conditions. Here we show that αB-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 β4–β8 groove of αB-crystallin. Such an interaction requires FAK tyrosine 925 and is enhanced following its phosphorylation by Src, which occurs upon FAK stimulation. αB-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 αB-crystallin against the stretch-induced apoptosis. Consistently, load-induced apoptosis is blunted in the hearts from cardiac-specific FAK transgenic mice transiently depleted of αB-crystallin by RNA interference. These studies define a role for αB-crystallin in controlling FAK function and cardiomyocyte survival through the prevention of calpain-mediated degradation of FAK.

Date: 2014
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DOI: 10.1038/ncomms6159

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