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dc.contributor.authorYang, Y
dc.contributor.authorWillis, TL
dc.contributor.authorButton, RW
dc.contributor.authorStrang, CJ
dc.contributor.authorFu, Y
dc.contributor.authorWen, X
dc.contributor.authorGrayson, PRC
dc.contributor.authorEvans, T
dc.contributor.authorSipthorpe, RJ
dc.contributor.authorRoberts, SL
dc.contributor.authorHu, B
dc.contributor.authorZhang, J
dc.contributor.authorLu, B
dc.contributor.authorLuo, S
dc.date.accessioned2019-08-21T19:59:02Z
dc.date.available2019-08-21T19:59:02Z
dc.date.issued2019-08-21
dc.identifier.issn2041-1723
dc.identifier.issn2041-1723
dc.identifier.other3759
dc.identifier.urihttp://hdl.handle.net/10026.1/14808
dc.description.abstract

<jats:title>Abstract</jats:title><jats:p>Autophagy cargo recognition and clearance are essential for intracellular protein quality control. SQSTM1/p62 sequesters intracellular aberrant proteins and mediates cargo delivery for their selective autophagic degradation. The formation of p62 non-membrane-bound liquid compartments is critical for its function as a cargo receptor. The regulation of p62 phase separation/condensation has yet been poorly characterised. Using an unbiased yeast two-hybrid screening and complementary approaches, we found that DAXX physically interacts with p62. Cytoplasmic DAXX promotes p62 puncta formation. We further elucidate that DAXX drives p62 liquid phase condensation by inducing p62 oligomerisation. This effect promotes p62 recruitment of Keap1 and subsequent Nrf2-mediated stress response. The present study suggests a mechanism of p62 phase condensation by a protein interaction, and indicates that DAXX regulates redox homoeostasis, providing a mechanistic insight into the prosurvival function of DAXX.</jats:p>

dc.format.extent0-0
dc.format.mediumElectronic
dc.languageen
dc.language.isoen
dc.publisherSpringer Science and Business Media LLC
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAnimals
dc.subjectAutophagy
dc.subjectCell Line
dc.subjectCo-Repressor Proteins
dc.subjectCytoplasm
dc.subjectDrosophila
dc.subjectFemale
dc.subjectGene Knockdown Techniques
dc.subjectHEK293 Cells
dc.subjectHeLa Cells
dc.subjectHumans
dc.subjectKelch-Like ECH-Associated Protein 1
dc.subjectMale
dc.subjectMice
dc.subjectMolecular Chaperones
dc.subjectNF-E2-Related Factor 2
dc.subjectNuclear Proteins
dc.subjectProtein Binding
dc.subjectProtein Folding
dc.subjectProtein Interaction Domains and Motifs
dc.subjectRNA-Binding Proteins
dc.subjectSequestosome-1 Protein
dc.titleCytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
dc.typejournal-article
dc.typeArticle
plymouth.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/31434890
plymouth.issue1
plymouth.volume10
plymouth.publisher-urlhttp://dx.doi.org/10.1038/s41467-019-11671-2
plymouth.publication-statusPublished online
plymouth.journalNature Communications
dc.identifier.doi10.1038/s41467-019-11671-2
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/Faculty of Health
plymouth.organisational-group/Plymouth/Faculty of Health/Peninsula Dental School
plymouth.organisational-group/Plymouth/Faculty of Health/Peninsula Medical School
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA03 Allied Health Professions, Dentistry, Nursing and Pharmacy
plymouth.organisational-group/Plymouth/Research Groups
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)/CBR
plymouth.organisational-group/Plymouth/Users by role
plymouth.organisational-group/Plymouth/Users by role/Academics
plymouth.organisational-group/Plymouth/Users by role/Researchers in ResearchFish submission
dc.publisher.placeEngland
dcterms.dateAccepted2019-07-18
dc.rights.embargodate2019-12-18
dc.identifier.eissn2041-1723
dc.rights.embargoperiodNot known
rioxxterms.versionofrecord10.1038/s41467-019-11671-2
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2019-08-21
rioxxterms.typeJournal Article/Review
plymouth.funderRole of the FoxN1 gene as a central regulator of epidermal planar cell polarity signaling expression and function::BBSRC
plymouth.funderRole of the FoxN1 gene as a central regulator of epidermal planar cell polarity signaling expression and function::BBSRC
plymouth.funderRole of the FoxN1 gene as a central regulator of epidermal planar cell polarity signaling expression and function::BBSRC
plymouth.funderRole of the FoxN1 gene as a central regulator of epidermal planar cell polarity signaling expression and function::BBSRC


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