Ca 2+ signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca 2+ channels

Handle URI:
http://hdl.handle.net/10754/561588
Title:
Ca 2+ signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca 2+ channels
Authors:
Qia, Zhi; Verma, Rajeev K.; Gehring, Christoph A. ( 0000-0003-4355-4591 ) ; Yamaguchi, Yube; Zhao, Yichen; Ryan, Clarence A.; Berkowitz, Gerald A.
Abstract:
A family of peptide signaling molecules (AtPeps) and their plasma membrane receptor AtPepR1 are known to act in pathogendefense signaling cascades in plants. Little is currently known about the molecular mechanisms that link these signaling peptides and their receptor, a leucine-rich repeat receptor-like kinase, to downstream pathogen-defense responses. We identify some cellular activities of these molecules that provide the context for a model for their action in signaling cascades. AtPeps activate plasma membrane inwardly conducting Ca 2+ permeable channels in mesophyll cells, resulting in cytosolic Ca 2+ elevation. This activity is dependent on their receptor as well as a cyclic nucleotide-gated channel (CNGC2). We also show that the leucine-rich repeat receptor- like kinase receptor AtPepR1 has guanylyl cyclase activity, generating cGMP from GTP, and that cGMP can activate CNGC2- dependent cytosolic Ca 2+ elevation. AtPep-dependent expression of pathogen-defense genes (PDF1.2, MPK3, and WRKY33) is mediated by the Ca 2+ signaling pathway associated with AtPep peptides and their receptor. The work presented here indicates that extracellular AtPeps, which can act as danger-associated molecular patterns, signal by interaction with their receptor, AtPepR1, a plasma membrane protein that can generate cGMP. Downstream from AtPep and AtPepR1 in a signaling cascade, the cGMP-activated channel CNGC2 is involved in AtPep- and AtPepR1-dependent inward Ca 2+ conductance and resulting cytosolic Ca 2+ elevation. The signaling cascade initiated by AtPeps leads to expression of pathogen- defense genes in a Ca 2+-dependent manner.
KAUST Department:
Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Molecular Signalling Group
Publisher:
National Academy of Sciences
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Issue Date:
18-Nov-2010
DOI:
10.1073/pnas.1000191107
PubMed ID:
21088220
PubMed Central ID:
PMC3000296
Type:
Article
ISSN:
00278424
Sponsors:
We thank Dr. Kiyoshi Masuda (Hokkaido University, Sapporo, Japan) for use of the real-time quantitative PCR machine, Dr. Gregory Pearce (Washington State University, Pullman, WA) for generating AtPep peptides, and Dr. Wei-Hua Wu (China Agriculture University, Beijing, China) for use of patch clamp equipment for some experiments. This work was supported by National Science Foundation Award 0844715 (to G. A. B.). Some work by Z.Q. was supported by a Program of Higher-Level Talents of Inner Mongolia University award (to Z.Q.).
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3000296
Appears in Collections:
Articles; Bioscience Program; Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorQia, Zhien
dc.contributor.authorVerma, Rajeev K.en
dc.contributor.authorGehring, Christoph A.en
dc.contributor.authorYamaguchi, Yubeen
dc.contributor.authorZhao, Yichenen
dc.contributor.authorRyan, Clarence A.en
dc.contributor.authorBerkowitz, Gerald A.en
dc.date.accessioned2015-08-02T09:14:50Zen
dc.date.available2015-08-02T09:14:50Zen
dc.date.issued2010-11-18en
dc.identifier.issn00278424en
dc.identifier.pmid21088220en
dc.identifier.doi10.1073/pnas.1000191107en
dc.identifier.urihttp://hdl.handle.net/10754/561588en
dc.description.abstractA family of peptide signaling molecules (AtPeps) and their plasma membrane receptor AtPepR1 are known to act in pathogendefense signaling cascades in plants. Little is currently known about the molecular mechanisms that link these signaling peptides and their receptor, a leucine-rich repeat receptor-like kinase, to downstream pathogen-defense responses. We identify some cellular activities of these molecules that provide the context for a model for their action in signaling cascades. AtPeps activate plasma membrane inwardly conducting Ca 2+ permeable channels in mesophyll cells, resulting in cytosolic Ca 2+ elevation. This activity is dependent on their receptor as well as a cyclic nucleotide-gated channel (CNGC2). We also show that the leucine-rich repeat receptor- like kinase receptor AtPepR1 has guanylyl cyclase activity, generating cGMP from GTP, and that cGMP can activate CNGC2- dependent cytosolic Ca 2+ elevation. AtPep-dependent expression of pathogen-defense genes (PDF1.2, MPK3, and WRKY33) is mediated by the Ca 2+ signaling pathway associated with AtPep peptides and their receptor. The work presented here indicates that extracellular AtPeps, which can act as danger-associated molecular patterns, signal by interaction with their receptor, AtPepR1, a plasma membrane protein that can generate cGMP. Downstream from AtPep and AtPepR1 in a signaling cascade, the cGMP-activated channel CNGC2 is involved in AtPep- and AtPepR1-dependent inward Ca 2+ conductance and resulting cytosolic Ca 2+ elevation. The signaling cascade initiated by AtPeps leads to expression of pathogen- defense genes in a Ca 2+-dependent manner.en
dc.description.sponsorshipWe thank Dr. Kiyoshi Masuda (Hokkaido University, Sapporo, Japan) for use of the real-time quantitative PCR machine, Dr. Gregory Pearce (Washington State University, Pullman, WA) for generating AtPep peptides, and Dr. Wei-Hua Wu (China Agriculture University, Beijing, China) for use of patch clamp equipment for some experiments. This work was supported by National Science Foundation Award 0844715 (to G. A. B.). Some work by Z.Q. was supported by a Program of Higher-Level Talents of Inner Mongolia University award (to Z.Q.).en
dc.publisherNational Academy of Sciencesen
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3000296en
dc.subjectBrassinosteroid associated kinase 1en
dc.subjectCalcium signalingen
dc.subjectFlagellin receptor 2en
dc.subjectPlant innate immunityen
dc.titleCa 2+ signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca 2+ channelsen
dc.typeArticleen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentMolecular Signalling Groupen
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaen
dc.identifier.pmcidPMC3000296en
dc.contributor.institutionCollege of Life Science, Inner Mongolia University, Hohhot, 010021, Chinaen
dc.contributor.institutionAgricultural Biotechnology Laboratory, Department of Plant Science, University of Connecticut, Storrs, CT 06269-4163, United Statesen
dc.contributor.institutionCrop Physiology Laboratory, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japanen
dc.contributor.institutionInstitute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, United Statesen
kaust.authorGehring, Christoph A.en

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