SAMM50 acts with p62 in piecemeal basal- and OXPHOS-induced mitophagy of SAM and MICOS components-Reference-Cited by-同舟云学术

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

Published:2021-05-26 Issue:8 Volume:220 Page:
ISSN:0021-9525
Container-title:Journal of Cell Biology
language:en
Short-container-title:

Author:

Abudu Yakubu Princely¹^ORCID,Shrestha Birendra Kumar¹^ORCID,Zhang Wenxin²,Palara Anthimi¹,Brenne Hanne Britt¹,Larsen Kenneth Bowitz¹^ORCID,Wolfson Deanna Lynn³^ORCID,Dumitriu Gianina⁴,Øie Cristina Ionica⁴,Ahluwalia Balpreet Singh³^ORCID,Levy Gahl⁴,Behrends Christian⁵⁶^ORCID,Tooze Sharon A.²^ORCID,Mouilleron Stephane⁷,Lamark Trond¹^ORCID,Johansen Terje¹^ORCID

Affiliation:

1. Molecular Cancer Research Group, Department of Medical Biology, University of Tromsø–The Arctic University of Norway, Tromsø, Norway

2. Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London, UK

3. Department of Physics and Technology, University of Tromsø–The Arctic University of Norway, Tromsø, Norway

4. Vascular Biology Research Group, Department of Medical Biology, University of Tromsø–The Arctic University of Norway, Tromsø, Norway

5. Institute of Biochemistry II, Goethe University Hospital, Frankfurt am Main, Germany

6. Munich Cluster for Systems Neurology (SyNergy), Ludwig Maximilian University, Munich, Germany

7. Structural Biology Science Technology Platform, The Francis Crick Institute, London, UK

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.

Funder

Norwegian Cancer Society

Research Council of Norway

Francis Crick Institute

Cancer Research UK

Medical Research Council

Wellcome Trust

Publisher

Rockefeller University Press

Subject

Cell Biology

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