English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/12516
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3

AuthorsSánchez-Barrena, María José ; Fujii, Hiroaki; Angulo, Iván ; Martínez-Ripoll, Martín ; Zhu, Jian-Kang; Albert, Armando
KeywordsAtSOS3
Protein kinases
Issue Date11-May-2007
PublisherElsevier
CitationMolecular Cell (2007) 26, 427-435
AbstractThe plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding calcium signals elicited by different environmental stimuli. SOS2 is activated by Ca-SOS3 and subsequently phosphorylates the ion transporter SOS1 to bring about cellular ion homeostasis under salt stress. In addition to possessing the kinase activity, members of the SOS2 family of protein kinases can bind to protein phosphatase 2Cs. The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS2 as a kinase and a phosphatase-binding protein. A comparison with the structure of unbound SOS3 reveals the basis of the molecular function of this family of kinases and their interacting calcium sensors. Furthermore, our study suggests that the structure of the phosphataseinteraction domain of SOS2 defines a scaffold module conserved from yeast to human.
DescriptionDisponible en: http://www.xtal.iqfr.csic.es/publications/molcell2007.pdf
Publisher version (URL)http://dx.doi.org/10.1016/j.molcel.2007.04.013
URIhttp://hdl.handle.net/10261/12516
DOI10.1016/j.molcel.2007.04.013
ISSN1097-2765
Appears in Collections:(IQFR) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.