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Título:	Lipid binding by the unique and SH3 domains of c-Src suggests a new regulation mechanism
Autor/a:	Pérez, Yolanda; Mattei, Mariano; Igea, Ana; Amata, Irene; Gairí Tahull, Margarida; Nebreda, Àngel R.; Bernadó Peretó, Pau; Pons Vallès, Miquel
Otros autores:	Universitat de Barcelona
Abstract:	c-Src is a non-receptor tyrosine kinase involved in numerous signal transduction pathways. The kinase,SH3 and SH2 domains of c-Src are attached to the membrane-anchoring SH4 domain through the flexible Unique domain. Here we show intra- and intermolecular interactions involving the Unique and SH3 domains suggesting the presence of a previously unrecognized additional regulation layer in c-Src. We have characterized lipid binding by the Unique and SH3 domains, their intramolecular interaction and its allosteric modulation by a SH3-binding peptide or by Calcium-loaded calmodulin binding to the Unique domain. We also show reduced lipid binding following phosphorylation at conserved sites of the Unique domain. Finally, we show that injection of full-length c-Src with mutations that abolish lipid binding by the Unique domain causes a strong in vivo phenotype distinct from that of wild-type c-Src in a Xenopus oocyte model system, confirming the functional role of the Unique domain in c-Src regulation.
Materia(s):	-Proteïnes quinases -Lípids -Receptors cel·lulars -Regulació cel·lular -Lligands (Bioquímica) -Protein kinases -Lipids -Cell receptors -Cellular control mechanisms -Ligands (Biochemistry)
Derechos:	cc-by-nc-nd (c) Pérez, Yolanda et al., 2013 http://creativecommons.org/licenses/by-nc-nd/3.0/es
Tipo de documento:	Artículo Artículo - Versión publicada
Editor:	Nature Publishing Group
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