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Título: | Structural and mechanistic insights into the association of PKCα-C2 domain to PtdIns(4,5)P2 |
Autor: | Guerrero-Valero, Marta; Ferrer-Orta, Cristina CSIC ORCID ; Querol-Audí, Jordi CSIC ORCID; Marín-Vicente, Consuelo CSIC; Fita, Ignacio CSIC ORCID ; Gómez-Fernández, Juan C.; Verdaguer, Núria CSIC ORCID ; Corbalán-García, Senena | Palabras clave: | Calcium phosphoinositides Peripheral membrane proteins |
Fecha de publicación: | 21-abr-2009 | Editor: | National Academy of Sciences (U.S.) | Citación: | Proceedings of the National Academy of Sciences of the United States of America 106(16): 6603-6607 (2009) | Resumen: | 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. | Versión del editor: | http://dx.doi.org/10.1073/pnas.0813099106 | URI: | http://hdl.handle.net/10261/110200 | DOI: | 10.1073/pnas.0813099106 | Identificadores: | doi: 10.1073/pnas.0813099106 issn: 0027-8424 |
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