title: Splitting up the powerhouse: structural insights into the mechanism of mitochondrial fission.
abstract: Mitochondria are dynamic organelles whose shape is regulated by the opposing processes of fission and fusion, operating in conjunction with organelle distribution along the cytoskeleton. The importance of fission and fusion homeostasis has been highlighted by a number of disease states linked to mutations in proteins involved in regulating mitochondrial morphology, in addition to changes in mitochondrial dynamics in Alzheimer's, Huntington's and Parkinson's diseases. While a number of mitochondrial morphology proteins have been identified, how they co-ordinate to assemble the fission apparatus is not clear. In addition, while the master mediator of mitochondrial fission, dynamin-related protein 1, is conserved throughout evolution, the adaptor proteins involved in its mitochondrial recruitment are not. This review focuses on our current understanding of mitochondrial fission and the proteins that regulate this process in cell homeostasis, with a particular focus on the recent mechanistic insights based on protein structures.
authors.affiliation: La Trobe Institute for Molecular Sciences, La Trobe University, Melbourne, 3086, Australia.
authors.forename: Viviane
authors.initials: V
authors.lastname: Richter
authors.affiliation: La Trobe Institute for Molecular Sciences, La Trobe University, Melbourne, 3086, Australia.
authors.forename: Abeer P
authors.initials: AP
authors.lastname: Singh
authors.affiliation: La Trobe Institute for Molecular Sciences, La Trobe University, Melbourne, 3086, Australia.
authors.forename: Marc
authors.initials: M
authors.lastname: Kvansakul
authors.affiliation: Department of Biochemistry and Molecular Biology, Monash University, Melbourne, 3800, Australia. Michael.Ryan@monash.edu.
authors.forename: Michael T
authors.initials: MT
authors.lastname: Ryan
authors.affiliation: Department of Biochemistry and Molecular Biology, Monash University, Melbourne, 3800, Australia. laura.osellame@monash.edu.
authors.forename: Laura D
authors.initials: LD
authors.lastname: Osellame
mesh_terms: D002308:Cardiolipins / Q000378:metabolism; D034281:Dynamins; D004721:Endoplasmic Reticulum / Q000502:physiology*; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D006706:Homeostasis / Q000502:physiology*; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000378:metabolism*; D063154:Mitochondrial Dynamics / Q000502:physiology*; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D051179:Plakins / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000378:metabolism
chemical_list: D002308:Cardiolipins; D008869:Microtubule-Associated Proteins; D024101:Mitochondrial Proteins; D051179:Plakins; D017382:Reactive Oxygen Species; D020558:GTP Phosphohydrolases; C110768:DNM1L protein, human; D034281:Dynamins
keywords: Adaptors; Dynamin-related protein 1; Endoplasmic reticulum; Fission; Lipids; Mitochondria; Outer mitochondrial membrane