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Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling

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Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling

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dc.contributor.author Diaz, Maira es_ES
dc.contributor.author Sanchez-Barrena, Maria Jose es_ES
dc.contributor.author Gonzalez Rubio, Juana Maria es_ES
dc.contributor.author Rodríguez Solovey, Leisa Natacha es_ES
dc.contributor.author Fernández, Daniel es_ES
dc.contributor.author Antoni-Alandes, Regina es_ES
dc.contributor.author Yunta, Cristina es_ES
dc.contributor.author Belda Palazón, Borja es_ES
dc.contributor.author González Guzmán, Miguel es_ES
dc.contributor.author Peirats-Llobet, Marta es_ES
dc.contributor.author Menendez, Margarita es_ES
dc.contributor.author Boskovic, Jasminka es_ES
dc.contributor.author Marquez, Jose es_ES
dc.contributor.author Rodríguez Egea, Pedro Luís es_ES
dc.contributor.author Albert, Armando es_ES
dc.date.accessioned 2017-06-07T10:07:54Z
dc.date.available 2017-06-07T10:07:54Z
dc.date.issued 2016-01-19
dc.identifier.issn 0027-8424
dc.identifier.uri http://hdl.handle.net/10251/82507
dc.description.abstract [EN] Regulation of ion transport in plants is essential for cell function. Abiotic stress unbalances cell ion homeostasis, and plants tend to readjust it, regulating membrane transporters and channels. The plant hormone abscisic acid (ABA) and the second messenger Ca2+ are central in such processes, as they are involved in the regulation of protein kinases and phosphatases that control ion transport activity in response to environmental stimuli. The identification and characterization of the molecular mechanisms underlying the effect of ABA and Ca2+ signaling pathways on membrane function are central and could provide opportunities for crop improvement. The C2-domain ABA-related (CAR) family of small proteins is involved in the Ca2+-dependent recruitment of the pyrabactin resistance 1/PYR1like (PYR/PYL) ABA receptors to the membrane. However, to fully understand CAR function, it is necessary to define a molecular mechanism that integrates Ca2+ sensing, membrane interaction, and the recognition of the PYR/PYL interacting partners. We present structural and biochemical data showing that CARs are peripheral membrane proteins that functionally cluster on the membrane and generate strong positive membrane curvature in a Ca2+-dependent manner. These features represent a mechanism for the generation, stabilization, and/or specific recognition of membrane discontinuities. Such structures may act as signaling platforms involved in the recruitment of PYR/PYL receptors and other signaling components involved in cell responses to stress. es_ES
dc.description.sponsorship A.A. and J.A.M. thank the European Syncrotron Radiation Facility and EMBL for access to the synchrotron radiation source. This work was funded by Ministerio de Economia y Competitividad (MINECO) Grants BFU2014-59796-R (to A.A.), BFU2011-28184-C02 (to M.J.S.-B.), and BIO2014-52537-R (to P.L.R.) and Comunidad de Madrid Grant S2010/BMD-2457 (to A.A and M.M.). M.J.S.-B. is supported by Ramon y Cajal Contract RYC-2008-03449 from MINECO and M.D. by a fellowship from Senacyt-Ifarhu. Access to the High Throughput Crystallization facility at European Molecular Biology Laboratory (EMBL) Grenoble was supported by the European Community's Seventh Framework Programme through the Protein Production Platform project (P-CUBE) Grant 227764. en_EN
dc.language Inglés es_ES
dc.publisher National Academy of Sciences es_ES
dc.relation.ispartof Proceedings of the National Academy of Sciences es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Signaling es_ES
dc.subject ion transport es_ES
dc.subject Membrane biology es_ES
dc.subject Abiotic stress es_ES
dc.subject.classification MICROBIOLOGIA es_ES
dc.subject.classification BIOQUIMICA Y BIOLOGIA MOLECULAR es_ES
dc.title Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1073/pnas.1512779113
dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/227764/EU/Infrastructure for Protein Production Platforms/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//BFU2014-59796-R/ES/BASES ESTRUCTURALES DE LOS DETERMINANTES PRINCIPALES DE LA HOMEOSTASIS IONICA EN PLANTAS: AVANCES EN EL MECANISMO REGULADOR DEL TRANSPORTE Y COMPARTIMENTALIZACION IONICA/
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//BIO2014-52537-R/ES/REGULACION DE LA SEÑALIZACION DEL ABA MEDIANTE MECHANISMOS QUE AFECTAN LOCALIZACION SUBCELULAR, VIDA MEDIA Y ACTIVIDAD DE RECEPTORES PARA REFORZAR TOLERANCIA VEGETAL A SEQUIA/
dc.relation.projectID info:eu-repo/grantAgreement/CAM//S2010%2FBMD2457/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//RYC-2008-03449/ES/RYC-2008-03449/
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//BFU2011-28184-C02/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia es_ES
dc.description.bibliographicCitation Diaz, M.; Sanchez-Barrena, MJ.; Gonzalez Rubio, JM.; Rodríguez Solovey, LN.; Fernández, D.; Antoni-Alandes, R.; Yunta, C.... (2016). Calcium-dependent oligomerization of CAR proteins at cell membrane modulates ABA signaling. Proceedings of the National Academy of Sciences. 113(3):E396-E405. https://doi.org/10.1073/pnas.1512779113 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://doi.org/10.1073/pnas.1512779113 es_ES
dc.description.upvformatpinicio E396 es_ES
dc.description.upvformatpfin E405 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 113 es_ES
dc.description.issue 3 es_ES
dc.relation.senia 308292 es_ES
dc.identifier.pmcid PMC4725540
dc.contributor.funder Ministerio de Economía y Competitividad
dc.contributor.funder Comunidad de Madrid
dc.contributor.funder European Commission
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