Phospholipids alter activity and stability of mitochondrial membrane-bound ubiquitin ligase MARCH5.
Ontology highlight
ABSTRACT: Mitochondrial homeostasis is tightly controlled by ubiquitination. The mitochondrial integral membrane ubiquitin ligase MARCH5 is a crucial regulator of mitochondrial membrane fission, fusion, and disposal through mitophagy. In addition, the lipid composition of mitochondrial membranes can determine mitochondrial dynamics and organelle turnover. However, how lipids influence the ubiquitination processes that control mitochondrial homeostasis remains unknown. Here, we show that lipids common to the mitochondrial membranes interact with MARCH5 and affect its activity and stability depending on the lipid composition in vitro. As the only one of the tested lipids, cardiolipin binding to purified MARCH5 induces a significant decrease in thermal stability, whereas stabilisation increases the str
SUBMITTER: Merklinger L
PROVIDER: S-EPMC9034062 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
ACCESS DATA