Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/115790
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Structural basis of the regulatory mechanism of the plant CIPK family of protein kinases controlling ion homeostasis and abiotic stress |
Autor: | Chaves Sanjuán, Antonio CSIC ORCID; Sánchez-Barrena, María José CSIC ORCID; González-Rubio, Juana M. CSIC; Moreno, M. CSIC; Ragel, Paula CSIC ORCID; Jiménez, M.; Pardo, José M. CSIC ORCID ; Martínez-Ripoll, Martín CSIC ORCID; Quintero, Francisco J. CSIC ORCID ; Albert, Armando CSIC ORCID | Palabras clave: | Abiotic stress Signaling Ion transport |
Fecha de publicación: | 2014 | Editor: | National Academy of Sciences (U.S.) | Citación: | Proceedings of the National Academy of Sciences 111(42): E4532- E4541 (2014) | Resumen: | © 2014, National Academy of Sciences. All rights reserved. Plant cells have developed specific protective molecular machinery against environmental stresses. The family of CBL-interacting protein kinases (CIPK) and their interacting activators, the calcium sensors calcineurin B-like (CBLs), work together to decode calcium signals elicited by stress situations. The molecular basis of biological activation of CIPKs relies on the calcium-dependent interaction of a self-inhibitory NAF motif with a particular CBL, the phosphorylation of the activation loop by upstream kinases, and the subsequent phosphorylation of the CBL by the CIPK. We present the crystal structures of the NAF-truncated and pseudophosphorylated kinase domains of CIPK23 and CIPK24/SOS2. In addition, we provide biochemical data showing that although CIPK23 is intrinsically inactive and requires an external stimulation, CIPK24/SOS2 displays basal activity. This data correlates well with the observed conformation of the respective activation loops: Although the loop of CIPK23 is folded into a well-ordered structure that blocks the active site access to substrates, the loop of CIPK24/SOS2 protrudes out of the active site and allows catalysis. These structures together with biochemical and biophysical data show that CIPK kinase activity necessarily requires the coordinated releases of the activation loop from the active site and of the NAF motif from the nucleotide-binding site. Taken all together, we postulate the basis for a conserved calcium-dependent NAF-mediated regulation of CIPKs and a variable regulation by upstream kinases. | Descripción: | 10 páginas.-- 6 figuras.-- 77 referencias.-- This article contains supporting information online at http://www.pnas.org/lookup/suppl/doi:10.1073/pnas.1407610111/-/DCSupplemental Data deposition: The atomic coordinates have been deposited in the Protein Data Bank (PDB), www.pdb.org (PDB ID codes 4CZT, 4CZU, and 4D28). |
Versión del editor: | http://dx.doi.org/10.1073/pnas.1407610111 | URI: | http://hdl.handle.net/10261/115790 | DOI: | 10.1073/pnas.1407610111 | Identificadores: | doi: 10.1073/pnas.1407610111 issn: 1091-6490 |
Aparece en las colecciones: | (IQF) Artículos (IRNAS) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
49
checked on 09-abr-2024
SCOPUSTM
Citations
86
checked on 17-abr-2024
WEB OF SCIENCETM
Citations
84
checked on 29-feb-2024
Page view(s)
389
checked on 19-abr-2024
Download(s)
102
checked on 19-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.