Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components

Yakubu Princely Abudu, Birendra Kumar Shrestha, Wenxin Zhang, Anthimi Palara, Hanne Britt Brenne, Kenneth Bowitz Larsen, Deanna Lynn Wolfson, Gianina Dumitriu, Cristina Ionica Øie, Balpreet Singh Ahluwalia, Gahl Levy, Christian Behrends, Sharon A. Tooze, Stephane Mouilleron, Trond Lamark, Terje Johansen

Research output: Contribution to journalArticlepeer-review


Mitophagy is the degradation of surplus or damaged mitochondria by autophagy. In addition to programmed and stressinduced 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.

Original languageEnglish
Article numbere202009092
JournalJournal of Cell Biology
Issue number8
StatePublished - 22 Aug 2021
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2021 Abudu et al.

ASJC Scopus subject areas

  • Cell Biology


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