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

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...

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Detalles Bibliográficos
Autores principales: Abudu, Yakubu Princely, Shrestha, Birendra Kumar, Zhang, Wenxin, Palara, Anthimi, Brenne, Hanne Britt, Larsen, Kenneth Bowitz, Wolfson, Deanna Lynn, Dumitriu, Gianina, Øie, Cristina Ionica, Ahluwalia, Balpreet Singh, Levy, Gahl, Behrends, Christian, Tooze, Sharon A., Mouilleron, Stephane, Lamark, Trond, Johansen, Terje
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8160579/
https://www.ncbi.nlm.nih.gov/pubmed/34037656
http://dx.doi.org/10.1083/jcb.202009092
Descripción
Sumario: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.