C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Autor: | Alexander M. van der Bliek, Daniel A. Rube, Mauro D. Zappaterra, Arnaud M. Labrousse |
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Rok vydání: | 1999 |
Předmět: |
Dynamins
inorganic chemicals Mitochondrial intermembrane space Recombinant Fusion Proteins Translocase of the outer membrane Molecular Sequence Data Vesicular Transport Proteins Gene Expression macromolecular substances Biology environment and public health Mitochondrial apoptosis-induced channel Mitochondrial membrane transport protein Oogenesis Consensus Sequence Animals Drosophila Proteins Humans Cell Lineage RNA Messenger Caenorhabditis elegans Caenorhabditis elegans Proteins Inner mitochondrial membrane Molecular Biology Sequence Homology Amino Acid Gene Expression Profiling Muscles Neuropeptides Membrane Proteins Intracellular Membranes Cell Biology Mitochondrial carrier Mitochondria Cell biology Mutation Translocase of the inner membrane biology.protein Tetradecanoylphorbol Acetate Female Genes Lethal ATP–ADP translocase Cell Division |
Zdroj: | Molecular Cell. 4:815-826 |
ISSN: | 1097-2765 |
DOI: | 10.1016/s1097-2765(00)80391-3 |
Popis: | Little is known about the mechanism of mitochondrial division. We show here that mitochondria are disrupted by mutations in a C. elegans dynamin-related protein (DRP-1). Mutant DRP-1 causes the mitochondrial matrix to retract into large blebs that are both surrounded and connected by tubules of outer membrane. This indicates that scission of the mitochondrial outer membrane is inhibited, while scission of the inner membrane still occurs. Overexpressed wild-type DRP-1 causes mitochondria to become excessively fragmented, consistent with an active role in mitochondrial scission. DRP-1 fused to GFP is observed in spots on mitochondria where scission eventually occurs. These data indicate that wild-type DRP-1 contributes to the final stages of mitochondrial division by controlling scission of the mitochondrial outer membrane. |
Databáze: | OpenAIRE |
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