OPA1 functionally interacts with MIC60 but is dispensable for crista junction formation

FEBS Lett. 2016 Oct;590(19):3309-3322. doi: 10.1002/1873-3468.12384. Epub 2016 Sep 18.

Abstract

Remodeling of crista junctions (CJs) is observed in numerous human disorders and during apoptosis. The functional interplay of OPA1 and MIC60, two key players in this context, is unclear. We show that OPA1 modulates cristae morphology but is dispensable for CJ formation. MIC60 is strongly enriched at CJs, whereas OPA1 is distributed evenly across the inner membrane. MIC60 levels are increased in OPA1-/- cells which show increased cellular resistance to apoptosis induction. Endogenous OPA1 and MIC60 show a physical interaction. Overall, we suggest that the regulation of CJ remodeling during apoptosis is mediated via an interplay between OPA1 and MIC60.

Keywords: MICOS; Mitofilin; apoptosis; crista junction; mitochondria.

Publication types

  • Letter

MeSH terms

  • Animals
  • Apoptosis
  • Cell Line
  • GTP Phosphohydrolases / genetics
  • GTP Phosphohydrolases / metabolism*
  • HeLa Cells
  • Humans
  • Mice
  • Mice, Inbred C57BL
  • Mitochondrial Membranes / metabolism*
  • Mitochondrial Membranes / ultrastructure
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism*
  • Muscle Proteins / genetics
  • Muscle Proteins / metabolism*
  • Protein Binding

Substances

  • Mitochondrial Proteins
  • Muscle Proteins
  • mitofilin protein, mouse
  • GTP Phosphohydrolases
  • Opa1 protein, mouse