气候变化领域集成服务门户(CCPortal): Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28

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DOI	10.1073/pnas.2024272118
	Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28
	Bredow M.; Bender K.W.; Dingee A.J.; Holmes D.R.; Thomson A.; Ciren D.; Tanney C.A.S.; Dunning K.E.; Trujillo M.; Huber S.C.; Monaghan J.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:19
英文摘要	Calcium (Ca2+)-dependent protein kinases (CDPKs or CPKs) are a unique family of Ca2+sensor/kinase-effector proteins with diverse functions in plants. In Arabidopsis thaliana, CPK28 contributes to immune homeostasis by promoting degradation of the key immune signaling receptor-like cytoplasmic kinase BOTRYTIS-INDUCED KINASE 1 (BIK1) and additionally functions in vegetative-to-reproductive stage transition. How CPK28 controls these seemingly disparate pathways is unknown. Here, we identify a single phosphorylation site in the kinase domain of CPK28 (Ser318) that is differentially required for its function in immune homeostasis and stem elongation. We show that CPK28 undergoes intermolecular autophosphorylation on Ser318 and can additionally be transphosphorylated on this residue by BIK1. Analysis of several other phosphorylation sites demonstrates that Ser318 phosphorylation is uniquely required to prime CPK28 for Ca2+activation at physiological concentrations of Ca2+, possibly through stabilization of the Ca2+-bound active state as indicated by intrinsic fluorescence experiments. Together, our data indicate that phosphorylation of Ser318 is required for the activation of CPK28 at low intracellular [Ca2+] to prevent initiation of an immune response in the absence of infection. By comparison, phosphorylation of Ser318 is not required for stem elongation, indicating pathway-specific requirements for phosphorylation-based Ca2+-sensitivity priming. We additionally provide evidence for a conserved function for Ser318 phosphorylation in related group IV CDPKs, which holds promise for biotechnological applications by generating CDPK alleles that enhance resistance to microbial pathogens without consequences to yield. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Arabidopsis thaliana; Calcium signaling; CDPK; Phosphorylation; Plant immunity
语种	英语
scopus关键词	calcium; calcium dependent protein kinase 28; protein kinase; unclassified drug; Arabidopsis protein; BIK1 protein, Arabidopsis; calcium; calcium-dependent protein kinase; PBL1 protein, Arabidopsis; protein kinase; serine; Article; autophosphorylation; calcium cell level; cell membrane; confocal microscopy; conformation; controlled study; fluorescence analysis; immune response; immune system; immunoprecipitation; molecular cloning; nonhuman; phylogeny; plant growth; protein analysis; protein function; protein localization; protein phosphorylation; amino acid sequence; Arabidopsis; classification; gene expression regulation; genetics; immunoblotting; metabolism; mutation; phosphorylation; Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Calcium; Gene Expression Regulation, Plant; Immunoblotting; Microscopy, Confocal; Mutation; Phosphorylation; Phylogeny; Protein Kinases; Protein Serine-Threonine Kinases; Serine
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/251192
作者单位	Department of Biology, Queen's University, Kingston, ON K7L 3N6, Canada; Department of Plant Biology, School of Integrative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States; Department of Cell Biology, University of Freiburg, Freiburg, 79104, Germany
推荐引用方式 GB/T 7714	Bredow M.,Bender K.W.,Dingee A.J.,et al. Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28[J],2021,118(19).
APA	Bredow M..,Bender K.W..,Dingee A.J..,Holmes D.R..,Thomson A..,...&Monaghan J..(2021).Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America,118(19).
MLA	Bredow M.,et al."Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28".Proceedings of the National Academy of Sciences of the United States of America 118.19(2021).