Talita M. Marin
State University of Campinas
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Publication
Featured researches published by Talita M. Marin.
Circulation Research | 2008
Talita M. Marin; Carolina F.M.Z. Clemente; Aline Santos; Paty K. Picardi; Vinícius D. B. Pascoal; Iscia Lopes-Cendes; Mario J.A. Saad; Kleber G. Franchini
The aim of this study was to investigate whether Shp2 (Src homology region 2, phosphatase 2) controls focal adhesion kinase (FAK) activity and its trophic actions in cardiomyocytes. We show that low phosphorylation levels of FAK in nonstretched neonatal rat ventricular myocytes (NRVMs) coincided with a relatively high basal association of FAK with Shp2 and Shp2 phosphatase activity. Cyclic stretch (15% above initial length) enhanced FAK phosphorylation at Tyr397 and reduced FAK/Shp2 association and phosphatase activity in anti-Shp2 precipitates. Recombinant Shp2 C-terminal protein tyrosine phosphatase domain (Shp2-PTP) interacted with nonphosphorylated recombinant FAK and dephosphorylated FAK immunoprecipitated from NRVMs. Depletion of Shp2 by specific small interfering RNA increased the phosphorylation of FAK Tyr397, Src Tyr418, AKT Ser473, TSC2 Thr1462, and S6 kinase Thr389 and induced hypertrophy of nonstretched NRVMs. Inhibition of FAK/Src activity by PP2 {4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine} abolished the phosphorylation of AKT, TSC2, and S6 kinase, as well as the hypertrophy of NRVMs induced by Shp2 depletion. Inhibition of mTOR (mammalian target of rapamycin) with rapamycin blunted the hypertrophy in NRVMs depleted of Shp2. NRVMs treated with PP2 or depleted of FAK by specific small interfering RNA were defective in FAK, Src, extracellular signal-regulated kinase, AKT, TSC2, and S6 kinase phosphorylation, as well as in the hypertrophic response to prolonged stretch. The stretch-induced hypertrophy of NRVMs was also prevented by rapamycin. These findings demonstrate that basal Shp2 tyrosine phosphatase activity controls the size of cardiomyocytes by downregulating a pathway that involves FAK/Src and mTOR signaling pathways.
FEBS Letters | 2009
Michel Vaz de Oliveira; Talita M. Marin; Carolina F.M.Z. Clemente; Ana Paula Dalla Costa; Carla C. Judice; Kleber G. Franchini
MINT‐7258938: Fak1 (uniprotkb:P34152) physically interacts (MI:0915) with shp2 (uniprotkb:P35235) by anti bait coimmunoprecipitation (MI:0006)
Brazilian Journal of Medical and Biological Research | 2009
Kleber G. Franchini; Carolina F.M.Z. Clemente; Talita M. Marin
Focal adhesion kinase (FAK) is a broadly expressed tyrosine kinase implicated in cellular functions such as migration, growth and survival. Emerging data support a role for FAK in cardiac development, reactive hypertrophy and failure. Data reviewed here indicate that FAK plays a critical role at the cellular level in the responses of cardiomyocytes and cardiac fibroblasts to biomechanical stress and to hypertrophic agonists such as angiotensin II and endothelin. The signaling mechanisms regulated by FAK are discussed to provide insight into its role in the pathophysiology of cardiac hypertrophy and failure.
Nature Chemical Biology | 2012
Aline Santos; Deborah Schechtman; Alisson C Cardoso; Carolina F.M.Z. Clemente; Júlio C Silva; Mariana Fioramonte; Michelle B. M. Pereira; Talita M. Marin; Paulo Sergio Lopes de Oliveira; Ana Figueira; Saulo Henrique Pires de Oliveira; Iris L. Torriani; Fabio C. Gozzo; José Xavier Neto; Kleber G. Franchini
Focal adhesion kinase (FAK) regulates cellular processes that affect several aspects of development and disease. The FAK N-terminal FERM (4.1 protein-ezrin-radixin-moesin homology) domain, a compact clover-leaf structure, binds partner proteins and mediates intramolecular regulatory interactions. Combined chemical cross-linking coupled to MS, small-angle X-ray scattering, computational docking and mutational analyses showed that the FAK FERM domain has a molecular cleft (~998 Å(2)) that interacts with sarcomeric myosin, resulting in FAK inhibition. Accordingly, mutations in a unique short amino acid sequence of the FERM myosin cleft, FP-1, impaired the interaction with myosin and enhanced FAK activity in cardiomyocytes. An FP-1 decoy peptide selectively inhibited myosin interaction and increased FAK activity, promoting cardiomyocyte hypertrophy through activation of the AKT-mammalian target of rapamycin pathway. Our findings uncover an inhibitory interaction between the FAK FERM domain and sarcomeric myosin that presents potential opportunities to modulate the cardiac hypertrophic response through changes in FAK activity.
FEBS Letters | 2016
Danieli Cristina Gonçalves; Talita M. Marin; Michelle B. M. Pereira; Aline Santos; Adriana Franco Paes Leme; Kleber G. Franchini
The small heat shock protein αB‐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.
Journal of Clinical Investigation | 2011
Talita M. Marin; Kimberly Keith; Benjamin Ivor Davies; David A. Conner; Prajna Guha; Demetrios Kalaitzidis; Xue Wu; Jessica Lauriol; Bo Wang; Michael P. Bauer; Roderick T. Bronson; Kleber G. Franchini; Benjamin G. Neel; Maria I. Kontaridis
American Journal of Physiology-heart and Circulatory Physiology | 2005
Adriana Souza Torsoni; Talita M. Marin; Lício A. Velloso; Kleber G. Franchini
Cardiovascular Research | 2005
Wilson Nadruz; Marcus Alexandre Finzi Corat; Talita M. Marin; Gonçalo Amarante Guimarães Pereira; Kleber G. Franchini
Frontiers in bioscience (Elite edition) | 2009
Carla C. Judice; Talita M. Marin; Kleber G. Franchini
Vigilância Sanitária em Debate | 2018
Talita M. Marin; Eduardo Pagani