SAMM50 is a receptor for basal piecemeal mitophagy and acts with SQSTM1/p62 in OXPHOS-induced mitophagy. Issue 9 (2nd September 2021)

• Record Type: Journal Article
• Authors: Abudu, Yakubu Princely; Mouilleron, Stephane; Tooze, Sharon A.; Lamark, Trond; Johansen, Terje
• Is Part Of: Autophagy. Volume 17:Issue 9(2021)
• Page Start: 2656
• Page End: 2658
• Publication Date: 2021-09-02
• Subjects: Atg8 -- basal -- piecemeal mitophagy -- metabolic switch -- MICOS -- OXPHOS -- p62 -- SAMM50 -- SQSTM1; Autophagic vacuoles -- Periodicals; Apoptosis -- Periodicals; Cell death -- Periodicals; Lysosomes -- Periodicals; Degeneration (Pathology) -- Periodicals; Autophagy -- Periodicals; Cell Death -- Periodicals; Lysosomes -- Periodicals; Periodicals; 571.936
• DOI: 10.1080/15548627.2021.1953846
• Languages: English
• ISSNs: 1554-8627

Abstract

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.