Publication

Article Metrics

Citations


Online attention

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

DOI: 10.1083/jcb.202009092 DOI Help

Authors: Yakubu Princely Abudu (University of Tromsø–The Arctic University of Norway) , Birendra Kumar Shrestha (University of Tromsø–The Arctic University of Norway) , Wenxin Zhang (The Francis Crick Institute) , Anthimi Palara (University of Tromsø–The Arctic University of Norway) , Hanne Britt Brenne (University of Tromsø–The Arctic University of Norway) , Kenneth Bowitz Larsen (University of Tromsø–The Arctic University of Norway) , Deanna Lynn Wolfson (University of Tromsø–The Arctic University of Norway) , Gianina Dumitriu (University of Tromsø–The Arctic University of Norway) , Cristina Ionica Øie (University of Tromsø–The Arctic University of Norway) , Balpreet Singh Ahluwalia (University of Tromsø–The Arctic University of Norway) , Gahl Levy (University of Tromsø–The Arctic University of Norway) , Christian Behrends (Goethe University Hospital; Ludwig Maximilian University) , Sharon A. Tooze (The Francis Crick Institute) , Stephane Mouilleron (The Francis Crick Institute) , Trond Lamark (University of Tromsø–The Arctic University of Norway) , Terje Johansen (University of Tromsø–The Arctic University of Norway)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Cell Biology , VOL 220

State: Published (Approved)
Published: August 2021
Diamond Proposal Number(s): 18566

Abstract: 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.

Journal Keywords: Biochemistry; Cell death and autophagy

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Discipline Tags:

Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)