The structure of arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress
Embargo End Date2012-10-02
Permanent link to this recordhttp://hdl.handle.net/10754/561910
MetadataShow full item record
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.
CitationYunta, C., Martínez-Ripoll, M., Zhu, J.-K., & Albert, A. (2011). The Structure of Arabidopsis thaliana OST1 Provides Insights into the Kinase Regulation Mechanism in Response to Osmotic Stress. Journal of Molecular Biology, 414(1), 135–144. doi:10.1016/j.jmb.2011.09.041
SponsorsWe 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.
JournalJournal of Molecular Biology
PubMed Central IDPMC3593245
- The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis.
- Authors: Yoshida R, Umezawa T, Mizoguchi T, Takahashi S, Takahashi F, Shinozaki K
- Issue date: 2006 Feb 24
- A link between magnesium-chelatase H subunit and sucrose nonfermenting 1 (SNF1)-related protein kinase SnRK2.6/OST1 in Arabidopsis guard cell signalling in response to abscisic acid.
- Authors: Liang S, Lu K, Wu Z, Jiang SC, Yu YT, Bi C, Xin Q, Wang XF, Zhang DP
- Issue date: 2015 Oct
- Protein phosphatases 2C regulate the activation of the Snf1-related kinase OST1 by abscisic acid in Arabidopsis.
- Authors: Vlad F, Rubio S, Rodrigues A, Sirichandra C, Belin C, Robert N, Leung J, Rodriguez PL, Laurière C, Merlot S
- Issue date: 2009 Oct
- Identification of features regulating OST1 kinase activity and OST1 function in guard cells.
- Authors: Belin C, de Franco PO, Bourbousse C, Chaignepain S, Schmitter JM, Vavasseur A, Giraudat J, Barbier-Brygoo H, Thomine S
- Issue date: 2006 Aug
- The Arabidopsis ABA-activated kinase OST1 phosphorylates the bZIP transcription factor ABF3 and creates a 14-3-3 binding site involved in its turnover.
- Authors: Sirichandra C, Davanture M, Turk BE, Zivy M, Valot B, Leung J, Merlot S
- Issue date: 2010 Nov 10