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AtAIRP2 E3 ligase affects ABA and high-salinity responses by stimulating its ATP1/SDIRIP1 substrate turnover

DC FieldValueLanguage
dc.contributor.author유문영-
dc.date.accessioned2018-07-20T12:02:51Z-
dc.date.available2018-07-20T12:02:51Z-
dc.date.issued2017-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/161694-
dc.description.abstractAtAIRP2 is a cytosolic RING-type E3 ubiquitin ligase that positively regulates an abscisic acid (ABA) response in Arabidopsis (Arabidopsis thaliana). Yeast two-hybrid screening using AtAIRP2 as bait identified ATP1 (AtAIRP2 Target Protein1) as a substrate of AtAIRP2. ATP1 was found to be identical to SDIRIP1, which was reported recently to be a negative factor in ABA signaling and a target protein of the RING E3 ligase SDIR1. Accordingly, ATP1 was renamed ATP1/SDIRIP1. A specific interaction between AtAIRP2 and ATP1/SDIRIP1 and ubiquitination of ATP1/SDIRIP1 by AtAIRP2 were demonstrated in vitro and in planta. The turnover of ATP1/SDIRIP1 was regulated by AtAIRP2 in cell-free degradation and protoplast cotransfection assays. The ABA-mediated germination assay of 35S:ATP1/SDIRIP1-RNAi/atairp2 double mutant progeny revealed that ATP1/SDIRIP1 acts downstream of AtAIRP2. AtAIRP2 and SDIR1 reciprocally complemented the ABA- and salt-insensitive germination phenotypes of sdir1 and atairp2 mutants, respectively, indicating their combinatory roles in seed germination. Subcellular localization and bimolecular fluorescence complementation experiments in the presence of MG132, a 26S proteasome inhibitor, showed that AtAIRP2 and ATP1/SDIRIP1 were colocalized to the cytosolic spherical body, which lies in close proximity to the nucleus, in tobacco (Nicotiana benthamiana) leaf cells. The 26S proteasome subunits RPN12a and RPT1 and the molecular chaperones HSP70 and HSP101 were colocalized to these discrete punctae-like structures. These results raised the possibility that AtAIRP2 and ATP1/SDIRIP1 interact in the cytosolic spherical compartment. Collectively, our data suggest that the down-regulation of ATP1/SDIRIP1 by AtAIRP2 and SDIR1 RING E3 ubiquitin ligases is critical for ABA and high-salinity responses during germination in Arabidopsis.-
dc.description.statementOfResponsibilityrestriction-
dc.languageUnited States-
dc.publisher1532-2548-
dc.relation.isPartOfPlant Physiology-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAbscisic Acid/pharmacology*-
dc.subject.MESHArabidopsis/drug effects-
dc.subject.MESHArabidopsis/genetics-
dc.subject.MESHArabidopsis/metabolism*-
dc.subject.MESHArabidopsis Proteins/metabolism*-
dc.subject.MESHCell Compartmentation-
dc.subject.MESHCytosol/drug effects-
dc.subject.MESHCytosol/metabolism-
dc.subject.MESHDown-Regulation/genetics-
dc.subject.MESHEpistasis, Genetic/drug effects-
dc.subject.MESHGenetic Complementation Test-
dc.subject.MESHGermination/drug effects-
dc.subject.MESHModels, Biological-
dc.subject.MESHMolecular Chaperones/metabolism-
dc.subject.MESHPlant Epidermis/cytology-
dc.subject.MESHProteasome Endopeptidase Complex/metabolism-
dc.subject.MESHProtein Binding/drug effects-
dc.subject.MESHProtein Subunits/metabolism-
dc.subject.MESHProton-Translocating ATPases/metabolism*-
dc.subject.MESHSalinity*-
dc.subject.MESHSeeds/drug effects-
dc.subject.MESHSeeds/growth & development-
dc.subject.MESHSubcellular Fractions/metabolism-
dc.subject.MESHSubstrate Specificity/drug effects-
dc.subject.MESHTobacco/cytology-
dc.titleAtAIRP2 E3 ligase affects ABA and high-salinity responses by stimulating its ATP1/SDIRIP1 substrate turnover-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Pharmacology-
dc.contributor.googleauthorTae Rin Oh-
dc.contributor.googleauthorJong Hum Kim-
dc.contributor.googleauthorSeok Keun Cho-
dc.contributor.googleauthorMoon Young Ryu-
dc.contributor.googleauthorSeong Wook Yang-
dc.contributor.googleauthorWoo Taek Kim-
dc.identifier.doi10.1104/pp.17.00467-
dc.contributor.localIdA05366-
dc.relation.journalcodeJ03373-
dc.identifier.eissn0032-0889-
dc.identifier.pmid28626006-
dc.identifier.urlhttp://www.plantphysiol.org/content/174/4/2515.long-
dc.contributor.alternativeNameRyu, Moon Young-
dc.contributor.affiliatedAuthorRyu, Moon Young-
dc.citation.volume174-
dc.citation.number4-
dc.citation.startPage2515-
dc.citation.endPage2531-
dc.identifier.bibliographicCitationPlant Physiology, Vol.174(4) : 2515-2531, 2017-
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실)

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