Literature DB >> 34275433

SAMM50 is a receptor for basal piecemeal mitophagy and acts with SQSTM1/p62 in OXPHOS-induced mitophagy.

Yakubu Princely Abudu1, Stephane Mouilleron2, Sharon A Tooze3, Trond Lamark1, Terje Johansen1.   

Abstract

Mitophagy, 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.

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Keywords:  Atg8; MICOS; OXPHOS; SAMM50; SQSTM1; basal; metabolic switch; p62; piecemeal mitophagy

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Year:  2021        PMID: 34275433      PMCID: PMC8496526          DOI: 10.1080/15548627.2021.1953846

Source DB:  PubMed          Journal:  Autophagy        ISSN: 1554-8627            Impact factor:   13.391


  1 in total

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

Authors:  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
Journal:  J Cell Biol       Date:  2021-05-26       Impact factor: 10.539

  1 in total

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