caa a22 4500 606174907 CHVBK 20210128100740.0 cr unu---uuuuu 210128e20151001xx s 000 0 eng 10.1007/s00018-015-1950-y doi (NATIONALLICENCE)springer-10.1007/s00018-015-1950-y Splitting up the powerhouse: structural insights into the mechanism of mitochondrial fission [Elektronische Daten] [Viviane Richter, Abeer Singh, Marc Kvansakul, Michael Ryan, Laura Osellame] 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. Springer Basel, 2015 Mitochondria nationallicence Fission nationallicence Dynamin-related protein 1 nationallicence Adaptors nationallicence Lipids nationallicence Outer mitochondrial membrane nationallicence Endoplasmic reticulum nationallicence Richter Viviane La Trobe Institute for Molecular Sciences, La Trobe University, 3086, Melbourne, Australia aut Singh Abeer La Trobe Institute for Molecular Sciences, La Trobe University, 3086, Melbourne, Australia aut Kvansakul Marc La Trobe Institute for Molecular Sciences, La Trobe University, 3086, Melbourne, Australia aut Ryan Michael Department of Biochemistry and Molecular Biology, Monash University, 3800, Melbourne, Australia aut Osellame Laura Department of Biochemistry and Molecular Biology, Monash University, 3800, Melbourne, Australia aut Cellular and Molecular Life Sciences Springer Basel 72/19(2015-10-01), 3695-3707 1420-682X 72:19<3695 2015 72 18 https://doi.org/10.1007/s00018-015-1950-y text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-1950-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Richter Viviane La Trobe Institute for Molecular Sciences, La Trobe University, 3086, Melbourne, Australia aut NATIONALLICENCE 700 1- Singh Abeer La Trobe Institute for Molecular Sciences, La Trobe University, 3086, Melbourne, Australia aut NATIONALLICENCE 700 1- Kvansakul Marc La Trobe Institute for Molecular Sciences, La Trobe University, 3086, Melbourne, Australia aut NATIONALLICENCE 700 1- Ryan Michael Department of Biochemistry and Molecular Biology, Monash University, 3800, Melbourne, Australia aut NATIONALLICENCE 700 1- Osellame Laura Department of Biochemistry and Molecular Biology, Monash University, 3800, Melbourne, Australia aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/19(2015-10-01), 3695-3707 1420-682X 72:19<3695 2015 72 18