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dc.contributor.authorAbudu, Yakubu Princely
dc.contributor.authorMouilleron, Stephane
dc.contributor.authorTooze, Sharon A
dc.contributor.authorLamark, Trond
dc.contributor.authorJohansen, Terje
dc.date.accessioned2022-03-29T10:56:02Z
dc.date.available2022-03-29T10:56:02Z
dc.date.issued2021-07-18
dc.description.abstractMitophagy, the clearance of surplus or damaged mitochondria or mitochondrial parts by autophagy, is important for maintenance of cellular homeostasis. Whereas knowledge on programmed and stress-induced mitophagy is increasing, much less is known about mechanisms of basal mitophagy. Recently, we identified SAMM50 (SAMM50 sorting and assembly machinery component) as a receptor for piecemeal degradation of components of the sorting and assembly machinery (SAM) complex and mitochondrial contact site and cristae organizing system (MICOS) complexes. SAMM50 interacts directly with Atg8-family proteins through a canonical LIR motif and with SQSTM1/p62 to mediate basal piecemeal mitophagy. During a metabolic switch to oxidative phosphorylation (OXPHOS), SAMM50 cooperates with SQSTM1 to mediate efficient piecemeal mitophagy.en_US
dc.descriptionThis is an Accepted Manuscript of an article published by Taylor & Francis in Autophagy on 18.07.22, available online: http://www.tandfonline.com/https://doi.org/10.1080/15548627.2021.1953846.en_US
dc.identifier.citationAbudu YP, Mouilleron S, Tooze SA, Lamark T, Johansen T. SAMM50 is a receptor for basal piecemeal mitophagy and acts with SQSTM1/p62 in OXPHOS-induced mitophagy. Autophagy. 2021en_US
dc.identifier.cristinIDFRIDAID 1926308
dc.identifier.doi10.1080/15548627.2021.1953846
dc.identifier.issn1554-8627
dc.identifier.issn1554-8635
dc.identifier.urihttps://hdl.handle.net/10037/24622
dc.language.isoengen_US
dc.publisherTaylor & Francisen_US
dc.relation.journalAutophagy
dc.relation.projectIDNorges forskningsråd: 249884en_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2021 The Author(s)en_US
dc.titleSAMM50 is a receptor for basal piecemeal mitophagy and acts with SQSTM1/p62 in OXPHOS-induced mitophagyen_US
dc.type.versionacceptedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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