| Literature DB >> 34275433 |
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.Entities:
Keywords: Atg8; MICOS; OXPHOS; SAMM50; SQSTM1; basal; metabolic switch; p62; piecemeal mitophagy
Mesh:
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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