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http://hdl.handle.net/10261/110200
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dc.contributor.author | Guerrero-Valero, Marta | - |
dc.contributor.author | Ferrer-Orta, Cristina | - |
dc.contributor.author | Querol-Audí, Jordi | - |
dc.contributor.author | Marín-Vicente, Consuelo | - |
dc.contributor.author | Fita, Ignacio | - |
dc.contributor.author | Gómez-Fernández, Juan C. | - |
dc.contributor.author | Verdaguer, Núria | - |
dc.contributor.author | Corbalán-García, Senena | - |
dc.date.accessioned | 2015-02-04T09:50:30Z | - |
dc.date.available | 2015-02-04T09:50:30Z | - |
dc.date.issued | 2009-04-21 | - |
dc.identifier | doi: 10.1073/pnas.0813099106 | - |
dc.identifier | issn: 0027-8424 | - |
dc.identifier.citation | Proceedings of the National Academy of Sciences of the United States of America 106(16): 6603-6607 (2009) | - |
dc.identifier.uri | http://hdl.handle.net/10261/110200 | - |
dc.description.abstract | C2 domains are widely-spread protein signaling motifs that in classical PKCs act as Ca2+-binding modules. However, the molecular mechanisms of their targeting process at the plasma membrane remain poorly understood. Here, the crystal structure of PKCα-C2 domain in complex with Ca 2+, 1,2-dihexanoyl-sn-glycero-3-[phospho-L-serine] (PtdSer), and 1,2-diayl-sn-glycero-3-[phosphoinositol-4,5-bisphos-phate] [Ptdlns(4,5)P2] shows that PtdSer binds specifically to the calcium-binding region, whereas Ptdlns(4,5)P2 occupies the concave surface of strands β3 and β4. Strikingly, the structure reveals a Ptdlns(4,5)P2-C2 domain-binding mode in which the aromatic residues Tyr-195 and Trp-245 establish direct interactions with the phosphate moieties of the inositol ring. Mutations that abrogate Tyr-195 and Trp-245 recognition of Ptdlns(4,5)P2 severely impaired the ability of PKCα to localize to the plasma membrane. Notably, these residues are highly conserved among C2 domains of topology I, and a general mechanism of C2 domain-membrane docking mediated by Ptdlns(4,5)P 2 is presented. | - |
dc.description.sponsorship | Work in Murcia was supported by the Fundación Médica Mutua Madrileña, Fundación Ramón Areces, and Fundación Séneca 08700/PI/08 (to S.C.-G.), and Ministerio de Ciencia e Innovación Grants BFU2005-02482 and BFU2008-01010 (to J.G.-F.). Work in Barcelona was supported by Ministerio de Ciencia e Innovación Grants BFU2005-02376/BMC (to N.V.) and BFU2005-08686-C02-01 (to I.F.).Financial support was provided by the European Synchrotron Radiation Facility | - |
dc.publisher | National Academy of Sciences (U.S.) | - |
dc.rights | closedAccess | - |
dc.subject | Calcium phosphoinositides | - |
dc.subject | Peripheral membrane proteins | - |
dc.title | Structural and mechanistic insights into the association of PKCα-C2 domain to PtdIns(4,5)P2 | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1073/pnas.0813099106 | - |
dc.relation.publisherversion | http://dx.doi.org/10.1073/pnas.0813099106 | - |
dc.date.updated | 2015-02-04T09:50:30Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.identifier.pmid | 19346474 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
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