alpha B-Crystallin interacts and attenuates the tyrosine phosphatase activity of Shp2 in cardiomyocytes under mechanical stress

Autor(es)

Goncalves, Danieli C. ; Marin, Talita M. ; Pereira, Michelle B. M. ; Santos, Aline M. ; Leme, Adriana F. Paes ; Franchini, Kleber G.

• Tipo de documento: Artigo Científico
• Fonte: FEBS Letters; v. 590, n. 14, p. 2232-2240, JUL 2016.
• Citações Web of Science: 2

Resumo

The small heat shock protein alpha B-Crystallin (CryAB, HspB5) and SH2 domain-containing tyrosine phosphatase 2 (Shp2) are important molecules in heart response to pathophysiological stress. Here we show that CryAB interacts with and potentially regulates Shp2 catalytic activity in stretched cardiomyocytes. Such an interaction requires CryAB oligomer to attenuate Shp2 activation. Stretched cardiomyocytes show a robust CryAB/Shp2 association accompanied by a reduction in the Shp2 phosphatase activity. Accordingly, CryAB knock-down in cardiomyocytes enhances Shp2 activity induced by mechanical stress. These results revealed a new role for CryAB, as a modulator of Shp2 phosphatase activity during a functionally relevant stimulus in cardiomyocytes. (AU)

• Processo FAPESP: 13/05877-8 - Caracterização estrutural e funcional da interação entre a chaperona alfaB-Cristalina e a tirosino-fosfatase Shp2.
• Beneficiário: Danieli Cristina Gonçalves
• Modalidade de apoio: Bolsas no Brasil - Doutorado