ERMO3MVP1GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana 英文参考文献.docVIP

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ERMO3MVP1GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana 英文参考文献.doc

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ERMO3MVP1GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana 英文参考文献

ERMO3/MVP1/GOLD36IsInvolvedinaCellType-Specific MechanismforMaintainingERMorphologyin Arabidopsisthaliana RyoheiThomasNakano1,RyoMatsushima1¤a,AtsushiJ.Nagano1¤b,YoichiroFukao2, MasayukiFujiwara2,MakiKondo3,MikioNishimura3,IkukoHara-Nishimura1* 1DepartmentofBotany,GraduateSchoolofScience,KyotoUniversity,Kyoto,Japan,2GraduateSchoolofBiologicalSciences,NaraInstituteofScienceandTechnology, Ikoma,Japan,3DepartmentofCellBiology,NationalInstituteforBasicBiology,Okazaki,Japan Abstract The endoplasmic reticulum (ER) has a unique, network-like morphology. The ER structures are composed of tubules, cisternae,andthree-wayjunctions.Thismorphologyishighlyconservedamongeukaryotes,butthemolecularmechanism thatmaintainsERmorphologyhasnotyetbeenelucidated.Inaddition,certainBrassicaceaeplantsdevelopauniqueER- derived organelle called the ER body. This organelle accumulates large amounts of PYK10, a b-glucosidase, but its physiologicalfunctionsarestillobscure.Weaimedtoidentifyanovelfactorrequiredformaintainingthemorphologyofthe ER, including ER bodies, and employed a forward-genetic approach using transgenic Arabidopsis thaliana (GFP-h) with fluorescently-labeled ER. We isolated and investigated a mutant (designated endoplasmic reticulum morphology3, ermo3) withhugeaggregatesandabnormalpunctatestructuresofER.ERMO3encodesaGDSL-lipase/esterasefamilyprotein,also knownasMVP1.Here,weshowedthat,althoughERMO3/MVP1/GOLD36 wasexpressedubiquitously,themorphological defects of ermo3 were specifically seen in a certain type of cells where ER bodies developed. Coimmunoprecipitation analysiscombinedwithmassspectrometryrevealedthatERMO3/MVP1/GOLD36interactswiththePYK10complex,ahuge proteincomplexthatisthoughttobeimportantforERbody-relateddefensesystems.Wealsofoundthatthedepletionof transcriptionfactorNAI1,amasterregulatorforERbodyformation,suppressedtheformationofER-aggregatesinermo3 cells,suggestingthatNAI1expressionplaysanimportantroleintheabnormalaggregationofER.Ourresultssuggestthat ERMO3/