Sharpening the scissors: mitochondrial fission with aid.
Over the past 5 yr, research in mitochondrial morphology has advanced rapidly, mainly as a result of the identification of protein factors involved in mitochondrial fission and fusion. The pathological relevance of these processes becomes clear as apoptotic cell death evidently involves mitochondrial fission and fusion machinery. Although the mechanisms by which cells maintain mitochondrial morphology are now beginning to be understood, interrelation between mitochondrial function and morphology is still not clear. This review describes the recent progress made in mitochondrial fission studies and ventures to seek an intricate link between morphology and function of mitochondria.
Department of Anesthesiology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA. yisang_yoon@urmc.rochester.edu
Yisang
Y
Yoon
D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D003593:Cytoplasm / Q000378:metabolism; D034281:Dynamins / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D053078:Membrane Potential, Mitochondrial; D008565:Membrane Proteins / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000378:metabolism*; D008954:Models, Biological; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000737:chemistry
C476525:FIS1 protein, human; C503403:Fis1 protein, rat; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D020558:GTP Phosphohydrolases; D034281:Dynamins