2007FEBS LettersOpen access

New insights into mitochondrial fusion

Yan Zhang, David C. Chan

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Abstract

Fusion controls mitochondrial morphology and is important for normal mitochondrial function, including roles in respiration, development, and apoptosis. Key components of the mitochondrial fusion machinery have been identified, allowing an initial dissection of its molecular mechanism. Outer and inner membrane fusion events are coordinately coupled but are mechanistically distinct. Mitofusins are mitochondrial GTPases that likely mediate outer membrane fusion. The dynamin-related protein OPA1/Mgm1p is required for inner membrane fusion and maintenance of normal cristae structure. We highlight recent findings that have advanced our understanding of the mechanism, function, and regulation of mitochondrial fusion.

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Fusion controls mitochondrial morphology and is important for normal mitochondrial function, including roles in respiration, development, and apoptosis. Key components of the mitochondrial fusion machinery have been identified, allowing an initial dissection of its molecular mechanism. Outer and inner membrane fusion events are coordinately coupled but are mechanistically distinct. Mitofusins are mitochondrial GTPases that likely mediate outer membrane fusion. The dynamin-related protein OPA1/Mgm1p is required for inner membrane fusion and maintenance of normal cristae structure. We highlight recent findings that have advanced our understanding of the mechanism, function, and regulation of mitochondrial fusion.

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Available abstract

Fusion controls mitochondrial morphology and is important for normal mitochondrial function, including roles in respiration, development, and apoptosis. Key components of the mitochondrial fusion machinery have been identified, allowing an initial dissection of its molecular mechanism. Outer and inner membrane fusion events are coordinately coupled but are mechanistically distinct. Mitofusins are mitochondrial GTPases that likely mediate outer membrane fusion. The dynamin-related protein OPA1/Mgm1p is required for inner membrane fusion and maintenance of normal cristae structure. We highlight recent findings that have advanced our understanding of the mechanism, function, and regulation of mitochondrial fusion.

Key concepts: mitochondrial fusion, Cell biology, Translocase of the inner membrane, Mitochondrial fission, Mitochondrion, Lipid bilayer fusion, Inner mitochondrial membrane, Translocase of the outer membrane

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