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Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin
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Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin
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Journal Article
Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin
2017
Overview
Ban
et al.
show that optic atrophy 1 (OPA1) and cardiolipin mediate mitochondrial fusion. In contrast, a homotypic
trans
-OPA1 interaction independent of cardiolipin mediates membrane tethering to form mitochondrial cristae.
Mitochondria are highly dynamic organelles that undergo frequent fusion and fission. Optic atrophy 1 (OPA1) is an essential GTPase protein for both mitochondrial inner membrane (IM) fusion and cristae morphology
1
,
2
. Under mitochondria-stress conditions, membrane-anchored L-OPA1 is proteolytically cleaved to form peripheral S-OPA1, leading to the selection of damaged mitochondria for mitophagy
2
,
3
,
4
. However, molecular details of the selective mitochondrial fusion are less well understood. Here, we showed that L-OPA1 and cardiolipin (CL) cooperate in heterotypic mitochondrial IM fusion. We reconstituted an
in vitro
membrane fusion reaction using purified human L-OPA1 protein expressed in silkworm, and found that L-OPA1 on one side of the membrane and CL on the other side are sufficient for fusion. GTP-independent membrane tethering through L-OPA1 and CL primes the subsequent GTP-hydrolysis-dependent fusion, which can be modulated by the presence of S-OPA1. These results unveil the most minimal intracellular membrane fusion machinery. In contrast, independent of CL, a homotypic
trans
-OPA1 interaction mediates membrane tethering, thereby supporting the cristae structure. Thus, multiple OPA1 functions are modulated by local CL conditions for regulation of mitochondrial morphology and quality control.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Analysis
/ Animals
/ Animals, Genetically Modified
/ Atrophy
/ Cristae
/ Damage
/ Fission
/ GTP Phosphohydrolases - chemistry
/ GTP Phosphohydrolases - genetics
/ GTP Phosphohydrolases - metabolism
/ Guanosine Triphosphate - metabolism
/ Humans
/ letter
/ Mitochondrial Membranes - enzymology
/ Protein Interaction Domains and Motifs
/ Protein-protein interactions
/ Recombinant Proteins - metabolism
