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SAMM50 acts with p62 in piecemeal basal- and OXPHOS-induced mitophagy of SAM and MICOS components

Permanent link
https://hdl.handle.net/10037/24143
DOI
https://doi.org/10.1083/jcb.202009092
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Date
2021-05-26
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Author
Abudu, Yakubu Princely; Shrestha, Birendra Kumar; Zhang, Wenxin; Palara, Anthimi; Brenne, Hanne Britt; Larsen, Kenneth Bowitz; Wolfson, Deanna; Dumitriu, Gianina; Øie, Cristina Ionica; Ahluwalia, Balpreet Singh; Levy, Gahl; Behrends, Christian; Tooze, Sharon A; Mouilleron, Stephane; Lamark, Trond; Johansen, Terje
Abstract
Mitophagy is the degradation of surplus or damaged mitochondria by autophagy. In addition to programmed and stress-induced mitophagy, basal mitophagy processes exert organelle quality control. Here, we show that the sorting and assembly machinery (SAM) complex protein SAMM50 interacts directly with ATG8 family proteins and p62/SQSTM1 to act as a receptor for a basal mitophagy of components of the SAM and mitochondrial contact site and cristae organizing system (MICOS) complexes. SAMM50 regulates mitochondrial architecture by controlling formation and assembly of the MICOS complex decisive for normal cristae morphology and exerts quality control of MICOS components. To this end, SAMM50 recruits ATG8 family proteins through a canonical LIR motif and interacts with p62/SQSTM1 to mediate basal mitophagy of SAM and MICOS components. Upon metabolic switch to oxidative phosphorylation, SAMM50 and p62 cooperate to mediate efficient mitophagy.
Publisher
Rockefeller University Press
Citation
Abudu YP, Shrestha BK, Zhang W, Palara A, Brenne HB, Larsen KBL, Wolfson DL, Dumitriu GA, Øie CI, Ahluwalia BS, Levy G, Behrends C, Tooze SA, Mouilleron S, Lamark T, Johansen T. SAMM50 acts with p62 in piecemeal basal- and OXPHOS-induced mitophagy of SAM and MICOS components. Journal of Cell Biology. 2021;220(8)
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  • Artikler, rapporter og annet (medisinsk biologi) [1103]
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