Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/44749
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pérez, Yolanda | - |
dc.contributor.author | Mattei, Mariano | - |
dc.contributor.author | Igea, Ana | - |
dc.contributor.author | Amata, Irene | - |
dc.contributor.author | Gairí Tahull, Margarida | - |
dc.contributor.author | Nebreda, Àngel R. | - |
dc.contributor.author | Bernadó Peretó, Pau | - |
dc.contributor.author | Pons Vallès, Miquel | - |
dc.date.accessioned | 2013-07-12T09:17:35Z | - |
dc.date.available | 2013-07-12T09:17:35Z | - |
dc.date.issued | 2013-02-18 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/2445/44749 | - |
dc.description.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. | - |
dc.format.extent | 9 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | - |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/10.1038/srep0129 | - |
dc.relation.isformatof | Reproducció del document publicat a: http://dx.doi.org/10.1038/srep0129 | - |
dc.relation.ispartof | Scientific Reports, 2013, vol. 3, num. 1295 | - |
dc.relation.uri | http://dx.doi.org/10.1038/srep0129 | - |
dc.rights | cc-by-nc-nd (c) Pérez, Yolanda et al., 2013 | - |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es | - |
dc.source | Articles publicats en revistes (Química Inorgànica i Orgànica) | - |
dc.subject.classification | Proteïnes quinases | - |
dc.subject.classification | Lípids | - |
dc.subject.classification | Receptors cel·lulars | - |
dc.subject.classification | Regulació cel·lular | - |
dc.subject.classification | Lligands (Bioquímica) | - |
dc.subject.other | Protein kinases | - |
dc.subject.other | Lipids | - |
dc.subject.other | Cell receptors | - |
dc.subject.other | Cellular control mechanisms | - |
dc.subject.other | Ligands (Biochemistry) | - |
dc.title | Lipid binding by the unique and SH3 domains of c-Src suggests a new regulation mechanism | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 622875 | - |
dc.date.updated | 2013-07-12T09:17:35Z | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/261863/EU//BIO-NMR | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
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 | Size | Format | |
---|---|---|---|---|
622875.pdf | 1.73 MB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License