Please use this identifier to cite or link to this item:
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
Receptors cel·lulars
Regulació cel·lular
Lligands (Bioquímica)
Protein kinases
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:
It is part of: Scientific Reports, 2013, vol. 3, num. 1295
ISSN: 2045-2322
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)
Publicacions de projectes de recerca finançats per la UE

Files in This Item:
File Description SizeFormat 
622875.pdf1.73 MBAdobe PDFView/Open

This item is licensed under a Creative Commons License Creative Commons