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© Aurelien Bayot
Confocal micrograph of HeLa cells visulazed by indirect immunocytochemistry for mitochondria in green with an Anti-TOMM40 antibody and nuclei in blue with Dapi.
Publication : The Journal of cell biology

The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of cell biology - 10 Mar 2014

Anand R, Wai T, Baker MJ, Kladt N, Schauss AC, Rugarli E, Langer T

Link to Pubmed [PMID] – 24616225

J. Cell Biol. 2014 Mar;204(6):919-29

Mitochondrial fusion and structure depend on the dynamin-like GTPase OPA1, whose activity is regulated by proteolytic processing. Constitutive OPA1 cleavage by YME1L and OMA1 at two distinct sites leads to the accumulation of both long and short forms of OPA1 and maintains mitochondrial fusion. Stress-induced OPA1 processing by OMA1 converts OPA1 completely into short isoforms, inhibits fusion, and triggers mitochondrial fragmentation. Here, we have analyzed the function of different OPA1 forms in cells lacking YME1L, OMA1, or both. Unexpectedly, deletion of Oma1 restored mitochondrial tubulation, cristae morphogenesis, and apoptotic resistance in cells lacking YME1L. Long OPA1 forms were sufficient to mediate mitochondrial fusion in these cells. Expression of short OPA1 forms promoted mitochondrial fragmentation, which indicates that they are associated with fission. Consistently, GTPase-inactive, short OPA1 forms partially colocalize with ER-mitochondria contact sites and the mitochondrial fission machinery. Thus, OPA1 processing is dispensable for fusion but coordinates the dynamic behavior of mitochondria and is crucial for mitochondrial integrity and quality control.

https://www.ncbi.nlm.nih.gov/pubmed/24616225