SHP-2 regulates myogenesis by coupling to FAK signaling pathway

de Oliveira, Michel V.; Marin, Talita M.; Clemente, Carolina F.; Costa, Ana Paula Dalla; Judice, Carla C.; Franchini, Kleber G.

doi:10.1016/j.febslet.2009.08.022

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Volume 583, Issue 18 , Pages 2975-2981, 17 September 2009

SHP-2 regulates myogenesis by coupling to FAK signaling pathway

Edited by Berend Wieringa

Michel V. de Oliveira
- Department of Internal Medicine, School of Medicine State University of Campinas, Brazil
Talita M. Marin
- Department of Internal Medicine, School of Medicine State University of Campinas, Brazil
Carolina F. Clemente
- Department of Internal Medicine, School of Medicine State University of Campinas, Brazil
Ana Paula Dalla Costa
- Department of Internal Medicine, School of Medicine State University of Campinas, Brazil
Carla C. Judice
- Department of Internal Medicine, School of Medicine State University of Campinas, Brazil
Kleber G. Franchini
- Department of Internal Medicine, School of Medicine State University of Campinas, Brazil
- Center for Structural Molecular Biology, Brazilian Association for Synchrotron Light Technology, Campinas, SP, Brazil
- Corresponding author. Departamento de Clínica Médica, Faculdade de Ciências Médicas, Universidade Estadual de Campinas, Cidade Universitária “Zefferino Vaz”, 13081-970 Campinas, SP, Brazil. Fax: +55 19 3521 8951.

Received 6 May 2009; received in revised form 1 August 2009; accepted 11 August 2009. published online 19 August 2009.

Abstract

Transient dephosphorylation of FAK at Tyr-397 is required for cell cycle withdrawal early on during myogenesis. Here, we show that upon serum starvation of C2C12 myoblasts, FAK is transiently dephosphorylated in parallel with SHP-2 activation and association with FAK. SHP-2 knockdown by RNA interference suppressed the transient upregulation of SHP-2 and dephosphorylation of FAK during myogenesis. Furthermore, depletion of SHP-2 retarded the cell cycle withdrawal and the differentiation of serum-starved myoblasts into myotubes. These data provide a mechanistic basis for the reduction in FAK activity in differentiating myoblasts, indicating that myogenesis is critically triggered by FAK/SHP-2 complex.

Structured summary

MINT-7258938: Fak1 (uniprotkb:P34152) physically interacts (MI:0915) with shp2 (uniprotkb:P35235) by anti bait coimmunoprecipitation (MI:0006)

Keywords: Myogenesis, Skeletal muscle, Cell signaling, Cell proliferation, Cell differentiation