中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases

文献类型:期刊论文

作者Ng, Ley-Moy2,3; Soon, Fen-Fen2,3; Zhou, X. Edward2; West, Graham M.4; Kovach, Amanda2; Suino-Powell, Kelly M.2; Chalmers, Michael J.4; Li, Jun2,3; Yong, Eu-Leong3; Zhu, Jian-Kang1
刊名PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
出版日期2011-12-27
卷号108期号:52页码:21259-21264
ISSN号0027-8424
DOI10.1073/pnas.1118651109
文献子类Article
英文摘要Abscisic acid (ABA) is an essential hormone that controls plant growth, development, and responses to abiotic stresses. Central for ABA signaling is the ABA-mediated autoactivation of three monomeric Snf1-related kinases (SnRK2.2, -2.3, and -2.6). In the absence of ABA, SnRK2s are kept in an inactive state by forming physical complexes with type 2C protein phosphatases (PP2Cs). Upon relief of this inhibition, SnRK2 kinases can autoactivate through unknown mechanisms. Here, we report the crystal structures of full-length Arabidopsis thaliana SnRK2.3 and SnRK2.6 at 1.9- and 2.3-angstrom resolution, respectively. The structures, in combination with biochemical studies, reveal a two-step mechanism of intramolecular kinase activation that resembles the intermolecular activation of cyclin-dependent kinases. First, release of inhibition by PP2C allows the SnRK2s to become partially active because of an intramolecular stabilization of the catalytic domain by a conserved helix in the kinase regulatory domain. This stabilization enables SnRK2s to gain full activity by activation loop autophosphorylation. Autophosphorylation is more efficient in SnRK2.6, which has higher stability than SnRK2.3 and has well-structured activation loop phosphate acceptor sites that are positioned next to the catalytic site. Together, these data provide a structural framework that links ABA-mediated release of PP2C inhibition to activation of SnRK2 kinases.
WOS关键词ACTIVATED PROTEIN-KINASES ; OSMOTIC-STRESS ; MECHANISM ; ARABIDOPSIS ; DOMAIN ; PHOSPHORYLATION ; PHOSPHATASES ; BINDING ; FAMILY ; LOOP
资助项目Michigan Economic Development Corporation[00000000] ; Michigan Technology Tri-Corridor[00000000] ; Office of Science of the US Department of Energy[00000000] ; Jay and Betty Van Andel Foundation[00000000] ; Amway (China) Limited[00000000] ; National Institutes of Health[00000000] ; Singapore Biomedical Research Council[00000000] ; National University of Singapore Graduate School for Integrative Sciences and Engineering (NGS)[00000000]
WOS研究方向Science & Technology - Other Topics
语种英语
出版者NATL ACAD SCIENCES
WOS记录号WOS:000298479900076
源URL[http://119.78.100.183/handle/2S10ELR8/278299]  
专题药物靶标结构与功能中心
中科院受体结构与功能重点实验室
新药研究国家重点实验室
通讯作者Zhu, Jian-Kang
作者单位1.Purdue Univ, Dept Hort & Landscape Architecture, W Lafayette, IN 47907 USA;
2.Van Andel Res Inst, Lab Struct Sci, Grand Rapids, MI 49503 USA;
3.Natl Univ Singapore, Yong Loo Lin Sch Med, Natl Univ Hosp, Dept Obstet & Gynecol, Singapore 117595, Singapore;
4.Scripps Res Inst, Translat Res Inst, Dept Mol Therapeut, Jupiter, FL 33458 USA;
5.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, State Key Lab Drug Res,Ctr Struct & Funct Drug Ta, Shanghai 201203, Peoples R China
推荐引用方式
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Ng, Ley-Moy,Soon, Fen-Fen,Zhou, X. Edward,et al. Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2011,108(52):21259-21264.
APA Ng, Ley-Moy.,Soon, Fen-Fen.,Zhou, X. Edward.,West, Graham M..,Kovach, Amanda.,...&Xu, H. Eric.(2011).Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,108(52),21259-21264.
MLA Ng, Ley-Moy,et al."Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108.52(2011):21259-21264.

入库方式: OAI收割

来源:上海药物研究所

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