Abstract
Dynamin-related proteins (DRPs) can generate forces to remodel membranes. In cells, DRPs require additional proteins [DRP-associated proteins (DAPs)] to conduct their functions. To dissect the mechanistic role of a DAP, we used the yeast mitochondrial division machine as a model, which requires the DRP Dnm1, and two other proteins, Mdv1 and Fis1. Mdv1 played a postmitochondrial targeting role in division by specifically interacting and coassembling with the guanosine triphosphate-bound form of Dnm1. This regulated interaction nucleated and promoted the self-assembly of Dnm1 into helical structures, which drive membrane scission. The nucleation of DRP assembly probably represents a general regulatory strategy for this family of filament-forming proteins, similar to F-actin regulation.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adaptor Proteins, Signal Transducing / metabolism*
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GTP Phosphohydrolases / chemistry
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GTP Phosphohydrolases / genetics
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GTP Phosphohydrolases / metabolism*
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Guanosine Triphosphate / analogs & derivatives
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Guanosine Triphosphate / metabolism
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Intracellular Membranes / physiology
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Kinetics
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Liposomes / metabolism
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Mitochondria / physiology*
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Mitochondrial Proteins / chemistry
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Mitochondrial Proteins / genetics
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Mitochondrial Proteins / metabolism*
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Models, Biological
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Adaptor Proteins, Signal Transducing
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FIS1 protein, S cerevisiae
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Liposomes
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MDV1 protein, S cerevisiae
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Mitochondrial Proteins
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Saccharomyces cerevisiae Proteins
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5'-guanylylmethylenebisphosphonate
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Guanosine Triphosphate
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GTP Phosphohydrolases
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DNM1 protein, S cerevisiae