The structure of arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress

Handle URI:
http://hdl.handle.net/10754/561910
Title:
The structure of arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress
Authors:
Yunta, Cristina; Martínez-Ripoll, Martín; Zhu, Jian-Kang; Albert, Armando
Abstract:
SnRK [SNF1 (sucrose non-fermenting-1)-related protein kinase] 2.6 [open stomata 1 (OST1)] is well characterized at molecular and physiological levels to control stomata closure in response to water-deficit stress. OST1 is a member of a family of 10 protein kinases from Arabidopsis thaliana (SnRK2) that integrates abscisic acid (ABA)-dependent and ABA-independent signals to coordinate the cell response to osmotic stress. A subgroup of protein phosphatases type 2C binds OST1 and keeps the kinase dephosphorylated and inactive. Activation of OST1 relies on the ABA-dependent inhibition of the protein phosphatases type 2C and the subsequent self-phosphorylation of the kinase. The OST1 ABA-independent activation depends on a short sequence motif that is conserved among all the members of the SnRK2 family. However, little is known about the molecular mechanism underlying this regulation. The crystallographic structure of OST1 shows that ABA-independent regulation motif stabilizes the conformation of the kinase catalytically essential α C helix, and it provides the basis of the ABA-independent regulation mechanism for the SnRK2 family of protein kinases. © 2011 Elsevier Ltd. All rights reserved.
KAUST Department:
Center for Desert Agriculture
Publisher:
Elsevier
Journal:
Journal of Molecular Biology
Issue Date:
Nov-2011
DOI:
10.1016/j.jmb.2011.09.041
PubMed ID:
21983340
PubMed Central ID:
PMC3593245
Type:
Article
ISSN:
00222836
Sponsors:
We thank Dr. Laura Lagartera for the analytical ultracentrifugation data analysis, Dr. F. J. Quintero for the access to his laboratory and advice in the kinase activity measurements and Dr. John Klingler for critical reading of the manuscript. A.A. thanks the European Synchrotron Radiation Facility for the access to the synchrotron radiation source. This work was funded by the grant BFU2008-00368/BMC, BFU2001-25384 and "Factoria de Cristalizacion" Consolider-Ingenio 2010 of the Spanish "Plan Nacional" (Ministerio de Ciencia e Innovacion) to A.A.
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3593245
Appears in Collections:
Articles; Center for Desert Agriculture

Full metadata record

DC FieldValue Language
dc.contributor.authorYunta, Cristinaen
dc.contributor.authorMartínez-Ripoll, Martínen
dc.contributor.authorZhu, Jian-Kangen
dc.contributor.authorAlbert, Armandoen
dc.date.accessioned2015-08-03T09:33:53Zen
dc.date.available2015-08-03T09:33:53Zen
dc.date.issued2011-11en
dc.identifier.issn00222836en
dc.identifier.pmid21983340en
dc.identifier.doi10.1016/j.jmb.2011.09.041en
dc.identifier.urihttp://hdl.handle.net/10754/561910en
dc.description.abstractSnRK [SNF1 (sucrose non-fermenting-1)-related protein kinase] 2.6 [open stomata 1 (OST1)] is well characterized at molecular and physiological levels to control stomata closure in response to water-deficit stress. OST1 is a member of a family of 10 protein kinases from Arabidopsis thaliana (SnRK2) that integrates abscisic acid (ABA)-dependent and ABA-independent signals to coordinate the cell response to osmotic stress. A subgroup of protein phosphatases type 2C binds OST1 and keeps the kinase dephosphorylated and inactive. Activation of OST1 relies on the ABA-dependent inhibition of the protein phosphatases type 2C and the subsequent self-phosphorylation of the kinase. The OST1 ABA-independent activation depends on a short sequence motif that is conserved among all the members of the SnRK2 family. However, little is known about the molecular mechanism underlying this regulation. The crystallographic structure of OST1 shows that ABA-independent regulation motif stabilizes the conformation of the kinase catalytically essential α C helix, and it provides the basis of the ABA-independent regulation mechanism for the SnRK2 family of protein kinases. © 2011 Elsevier Ltd. All rights reserved.en
dc.description.sponsorshipWe thank Dr. Laura Lagartera for the analytical ultracentrifugation data analysis, Dr. F. J. Quintero for the access to his laboratory and advice in the kinase activity measurements and Dr. John Klingler for critical reading of the manuscript. A.A. thanks the European Synchrotron Radiation Facility for the access to the synchrotron radiation source. This work was funded by the grant BFU2008-00368/BMC, BFU2001-25384 and "Factoria de Cristalizacion" Consolider-Ingenio 2010 of the Spanish "Plan Nacional" (Ministerio de Ciencia e Innovacion) to A.A.en
dc.publisherElsevieren
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3593245en
dc.subjectcrystallographyen
dc.subjectkinase regulationen
dc.subjectplant abiotic stressen
dc.subjectprotein structureen
dc.subjectsignalingen
dc.titleThe structure of arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stressen
dc.typeArticleen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalJournal of Molecular Biologyen
dc.identifier.pmcidPMC3593245en
dc.contributor.institutionDepartamento de Cristalografía y Biología Estructural, Instituto de Química Física Rocasolano, Consejo Superior de Investigaciones Científicas, Serrano 119, Madrid E-28006, Spainen
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907, United Statesen
kaust.authorZhu, Jian-Kangen

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.