English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/125537
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Regulation of c-Src tyrosine kinase activity by calmodulin

AuthorsStateva, Silvia R.; Anguita, Estefanía; Salas, Valentina; Benaim, Gustavo; Villalobo, Antonio
Issue Date2014
PublisherSociedad Española de Bioquímica y Biología Molecular
CitationXXXVII Congreso SEBBM (2014)
AbstractCalmodulin (CaM) is a Ca2+-receptor protein that regulates more than one hundred target proteins with and without enzymatic activity in Ca2+- dependent and independent manners and modulates a myriad of cellular processes, some of which are vital for tumorigenesis (i.e. cell proliferation, apoptosis and autophagy). c-Src is a non-receptor tyrosine kinase that participates in signaling pathways that transduces events initiated by different types of cellular receptors and adhesion molecules, and controls many cellular functions including: cell migration, proliferation, differentiation, apoptosis and stress-response, among others. It has been previously demonstrated that CaM directly interacts with c-Src in a partial Ca2+-dependent manner and that trifl uoperazine, a CaM antagonist, inhibits the phosphorylation of c-Src, suggesting that CaM plays an important role in survival signals in pancreatic tumor cells. We demonstrate in this work that recombinant c-Src directly binds CaM in Ca2+-dependent and independent manners, suggesting that this kinase likely has more than one CaM-binding domain. A couple of IQ-like motifs identified in silico in c-Src could be responsible for the binding of CaM to this kinase in the absence of Ca2+. We also show that CaM enhances the autophosphorylation and tyrosine kinase activity of c-Src in the absence and presence of Ca2+, most strongly in the former condition. We are testing whether the CaM antagonist W-7 inhibits or not the hydrogen peroxideinduced phosphorylation of c-Src in human breast adenocarcinoma SKBR-3 cells, and whether or not CaM-dependent protein kinase II and/or the CaM-regulated protein phosphatase calcineurin, play a role in this process.
DescriptionResumen del póster presentado al XXXVII Congreso de la Sociedad Española de Bioquímica y Biología Molecular, celebrado en Granada del 9 al 12 de septiembre de 2014.
Appears in Collections:(IIBM) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.