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UXT chaperone prevents proteotoxicity by acting as an autophagy adaptor for p62-dependent aggrephagy

DC Field Value Language
dc.contributor.author옥지연-
dc.contributor.author정호성-
dc.date.accessioned2021-04-29T17:39:04Z-
dc.date.available2021-04-29T17:39:04Z-
dc.date.issued2021-03-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/182451-
dc.description.abstractp62/SQSTM1 is known to act as a key mediator in the selective autophagy of protein aggregates, or aggrephagy, by steering ubiquitinated protein aggregates towards the autophagy pathway. Here, we use a yeast two-hybrid screen to identify the prefoldin-like chaperone UXT as an interacting protein of p62. We show that UXT can bind to protein aggregates as well as the LB domain of p62, and, possibly by forming an oligomer, increase p62 clustering for its efficient targeting to protein aggregates, thereby promoting the formation of the p62 body and clearance of its cargo via autophagy. We also find that ectopic expression of human UXT delays SOD1(A4V)-induced degeneration of motor neurons in a Xenopus model system, and that specific disruption of the interaction between UXT and p62 suppresses UXT-mediated protection. Together, these results indicate that UXT functions as an autophagy adaptor of p62-dependent aggrephagy. Furthermore, our study illustrates a cooperative relationship between molecular chaperones and the aggrephagy machinery that efficiently removes misfolded protein aggregates.-
dc.description.statementOfResponsibilityopen-
dc.formatapplication/pdf-
dc.languageEnglish-
dc.publisherNature Pub. Group-
dc.relation.isPartOfNATURE COMMUNICATIONS-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.subject.MESHAnimals-
dc.subject.MESHAutophagy / drug effects-
dc.subject.MESHAutophagy / genetics*-
dc.subject.MESHCell Cycle Proteins / genetics*-
dc.subject.MESHCell Cycle Proteins / metabolism-
dc.subject.MESHGanglia, Spinal / cytology-
dc.subject.MESHGanglia, Spinal / metabolism-
dc.subject.MESHGene Expression Regulation-
dc.subject.MESHGenes, Reporter-
dc.subject.MESHGreen Fluorescent Proteins / genetics-
dc.subject.MESHGreen Fluorescent Proteins / metabolism-
dc.subject.MESHHEK293 Cells-
dc.subject.MESHHeLa Cells-
dc.subject.MESHHumans-
dc.subject.MESHLeupeptins / pharmacology-
dc.subject.MESHLuminescent Proteins / genetics-
dc.subject.MESHLuminescent Proteins / metabolism-
dc.subject.MESHMolecular Chaperones / genetics*-
dc.subject.MESHMolecular Chaperones / metabolism-
dc.subject.MESHMotor Neurons / cytology-
dc.subject.MESHMotor Neurons / drug effects-
dc.subject.MESHMotor Neurons / metabolism-
dc.subject.MESHPrimary Cell Culture-
dc.subject.MESHProteasome Endopeptidase Complex / drug effects-
dc.subject.MESHProteasome Endopeptidase Complex / metabolism-
dc.subject.MESHProtein Aggregates* / drug effects-
dc.subject.MESHProtein Folding / drug effects-
dc.subject.MESHSequestosome-1 Protein / genetics*-
dc.subject.MESHSequestosome-1 Protein / metabolism-
dc.subject.MESHSignal Transduction-
dc.subject.MESHSuperoxide Dismutase-1 / genetics*-
dc.subject.MESHSuperoxide Dismutase-1 / metabolism-
dc.subject.MESHTransgenes-
dc.subject.MESHXenopus laevis-
dc.titleUXT chaperone prevents proteotoxicity by acting as an autophagy adaptor for p62-dependent aggrephagy-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Anatomy (해부학교실)-
dc.contributor.googleauthorMin Ji Yoon-
dc.contributor.googleauthorBoyoon Choi-
dc.contributor.googleauthorEun Jin Kim-
dc.contributor.googleauthorJiyeon Ohk-
dc.contributor.googleauthorChansik Yang-
dc.contributor.googleauthorYeon-Gil Choi-
dc.contributor.googleauthorJinyoung Lee-
dc.contributor.googleauthorChanhee Kang-
dc.contributor.googleauthorHyun Kyu Song-
dc.contributor.googleauthorYoon Ki Kim-
dc.contributor.googleauthorJae-Sung Woo-
dc.contributor.googleauthorYongcheol Cho-
dc.contributor.googleauthorEui-Ju Choi-
dc.contributor.googleauthorHosung Jung-
dc.contributor.googleauthorChungho Kim-
dc.identifier.doi10.1038/s41467-021-22252-7-
dc.contributor.localIdA06051-
dc.contributor.localIdA03786-
dc.relation.journalcodeJ02293-
dc.identifier.eissn2041-1723-
dc.identifier.pmid33782410-
dc.contributor.alternativeNameOhk, Jiyeon-
dc.contributor.affiliatedAuthor옥지연-
dc.contributor.affiliatedAuthor정호성-
dc.citation.volume12-
dc.citation.number1-
dc.citation.startPage1955-
dc.identifier.bibliographicCitationNATURE COMMUNICATIONS, Vol.12(1) : 1955, 2021-03-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Anatomy (해부학교실) > 1. Journal Papers

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