Arabidopsis Chaperone J3 Regulates the Plasma Membrane H⁺-ATPase through Interaction with the PKS5 Kinase

The plasma membrane H⁺-ATPase (PM H⁺-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H⁺-ATPase activity is controlled by many factors, including hormon...

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Published in	The Plant cell Vol. 22; no. 4; pp. 1313 - 1332
Main Authors	Yang, Yongqing, Qin, Yunxia, Xie, Changgen, Zhao, Feiyi, Zhao, Jinfeng, Liu, Dafa, Chen, Shouyi, Fuglsang, Anja T, Palmgren, Michael G, Schumaker, Karen S, Deng, Xing Wang, Guo, Yan
Format	Journal Article
Language	English
Published	England American Society of Plant Biologists 01.04.2010
Subjects	alleles Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana calcium cell growth Cell membranes Gene expression regulation Gene Expression Regulation, Plant heat shock proteins hormones HSP40 Heat-Shock Proteins - genetics HSP40 Heat-Shock Proteins - metabolism Hydrogen-Ion Concentration ion transport Microscopy, Confocal mutants Mutation Plant cells Plant roots Plant Roots - metabolism Plants plasma membrane Plasmids Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Proteins Proton-Translocating ATPases - genetics Proton-Translocating ATPases - metabolism Protons RNA, Plant - genetics salts Seedlings Sodium Chloride - pharmacology soil salinity stomatal movement
Online Access	Get full text
ISSN	1040-4651 1532-298X 1532-298X
DOI	10.1105/tpc.109.069609

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Abstract	The plasma membrane H⁺-ATPase (PM H⁺-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H⁺-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H⁺-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H⁺-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H⁺-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H⁺-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H⁺-ATPase activity by J3 takes place via inactivation of the PKS5 kinase.
AbstractList	The plasma membrane H(+)-ATPase (PM H(+)-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H(+)-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H(+)-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H(+)-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H(+)-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H(+)-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H(+)-ATPase activity by J3 takes place via inactivation of the PKS5 kinase. The plasma membrane H⁺-ATPase (PM H⁺-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H⁺-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H⁺-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H⁺-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H⁺-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H⁺-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H⁺-ATPase activity by J3 takes place via inactivation of the PKS5 kinase. The plasma membrane H(+)-ATPase (PM H(+)-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H(+)-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H(+)-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H(+)-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H(+)-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H(+)-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H(+)-ATPase activity by J3 takes place via inactivation of the PKS5 kinase.The plasma membrane H(+)-ATPase (PM H(+)-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H(+)-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H(+)-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H(+)-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H(+)-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H(+)-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H(+)-ATPase activity by J3 takes place via inactivation of the PKS5 kinase. This work examines the effect of a DnaJ homolog, Arabidopsis J3, on the activity of the plasma membrane H + -ATPase, showing that J3 affects activity of the ATPase by direct interaction with and inactivation of a repressor protein kinase, Salt Overly Sensitive2-Like Protein Kinase5. The plasma membrane H + -ATPase (PM H + -ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H + -ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H + -ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H + -ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H + -ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H + -ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H + -ATPase activity by J3 takes place via inactivation of the PKS5 kinase.
Author	Deng, Xing Wang Guo, Yan Palmgren, Michael G Fuglsang, Anja T Xie, Changgen Liu, Dafa Qin, Yunxia Zhao, Jinfeng Yang, Yongqing Zhao, Feiyi Chen, Shouyi Schumaker, Karen S
AuthorAffiliation	e Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101 China c State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100094, China d Key Lab of Ministry of Agriculture for Biology of Rubber Tree, Rubber Research Institute, Chinese Academy of Tropical Agricultural Sciences, Danzhou, Hainan 571737, China f Department of Plant Biology, University of Copenhagen, DK-1871 Frederiksberg C, Denmark a College of Life Sciences, Peking University, Beijing 100871, China b National Institute of Biological Sciences, Beijing 102206, China g Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721
AuthorAffiliation_xml	– name: b National Institute of Biological Sciences, Beijing 102206, China – name: d Key Lab of Ministry of Agriculture for Biology of Rubber Tree, Rubber Research Institute, Chinese Academy of Tropical Agricultural Sciences, Danzhou, Hainan 571737, China – name: c State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100094, China – name: f Department of Plant Biology, University of Copenhagen, DK-1871 Frederiksberg C, Denmark – name: g Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721 – name: e Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101 China – name: a College of Life Sciences, Peking University, Beijing 100871, China
Author_xml	– sequence: 1 fullname: Yang, Yongqing – sequence: 2 fullname: Qin, Yunxia – sequence: 3 fullname: Xie, Changgen – sequence: 4 fullname: Zhao, Feiyi – sequence: 5 fullname: Zhao, Jinfeng – sequence: 6 fullname: Liu, Dafa – sequence: 7 fullname: Chen, Shouyi – sequence: 8 fullname: Fuglsang, Anja T – sequence: 9 fullname: Palmgren, Michael G – sequence: 10 fullname: Schumaker, Karen S – sequence: 11 fullname: Deng, Xing Wang – sequence: 12 fullname: Guo, Yan
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/20418496$$D View this record in MEDLINE/PubMed
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Copyright	2010 American Society of Plant Biologists 2010 American Society of Plant Biologists 2010
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Some figures in this article are displayed in color online but in black and white in the print edition. These authors contributed equally to this work. Online version contains Web-only data. www.plantcell.org/cgi/doi/10.1105/tpc.109.069609
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PublicationTitle	The Plant cell
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Snippet	The plasma membrane H⁺-ATPase (PM H⁺-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological... The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological... The plasma membrane H(+)-ATPase (PM H(+)-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological... This work examines the effect of a DnaJ homolog, Arabidopsis J3, on the activity of the plasma membrane H + -ATPase, showing that J3 affects activity of the...
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SubjectTerms	alleles Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana calcium cell growth Cell membranes Gene expression regulation Gene Expression Regulation, Plant heat shock proteins hormones HSP40 Heat-Shock Proteins - genetics HSP40 Heat-Shock Proteins - metabolism Hydrogen-Ion Concentration ion transport Microscopy, Confocal mutants Mutation Plant cells Plant roots Plant Roots - metabolism Plants plasma membrane Plasmids Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Proteins Proton-Translocating ATPases - genetics Proton-Translocating ATPases - metabolism Protons RNA, Plant - genetics salts Seedlings Sodium Chloride - pharmacology soil salinity stomatal movement
Title	Arabidopsis Chaperone J3 Regulates the Plasma Membrane H⁺-ATPase through Interaction with the PKS5 Kinase
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