SAMM50 is a receptor for basal piecemeal mitophagy and acts with SQSTM1/p62 in OXPHOS-induced mitophagy
Permanent lenke
https://hdl.handle.net/10037/24622Dato
2021-07-18Type
Journal articleTidsskriftartikkel
Peer reviewed
Forfatter
Abudu, Yakubu Princely; Mouilleron, Stephane; Tooze, Sharon A; Lamark, Trond; Johansen, TerjeSammendrag
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.
Beskrivelse
This is an Accepted Manuscript of an article published by Taylor & Francis in Autophagy on 18.07.22, available online: http://www.tandfonline.com/https://doi.org/10.1080/15548627.2021.1953846.
Forlag
Taylor & FrancisSitering
Abudu YP, Mouilleron S, Tooze SA, Lamark T, Johansen T. SAMM50 is a receptor for basal piecemeal mitophagy and acts with SQSTM1/p62 in OXPHOS-induced mitophagy. Autophagy. 2021Metadata
Vis full innførselSamlinger
Copyright 2021 The Author(s)