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Title: | Lipid binding by the unique and SH3 domains of c-Src suggests a new regulation mechanism |
Author: | Pérez, Yolanda Mattei, Mariano Igea, Ana Amata, Irene Gairí Tahull, Margarida Nebreda, Àngel R. Bernadó Peretó, Pau Pons Vallès, Miquel |
Keywords: | Proteïnes quinases Lípids Receptors cel·lulars Regulació cel·lular Lligands (Bioquímica) Protein kinases Lipids Cell receptors Cellular control mechanisms Ligands (Biochemistry) |
Issue Date: | 18-Feb-2013 |
Publisher: | Nature Publishing Group |
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. |
Note: | Reproducció del document publicat a: http://dx.doi.org/10.1038/srep0129 |
It is part of: | Scientific Reports, 2013, vol. 3, num. 1295 |
URI: | http://hdl.handle.net/2445/44749 |
Related resource: | http://dx.doi.org/10.1038/srep0129 |
ISSN: | 2045-2322 |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) Publicacions de projectes de recerca finançats per la UE |
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