Abstract
To initiate mitochondrial fission, dynamin-related proteins (DRPs) must bind specific adaptors on the outer mitochondrial membrane. The structural features underlying this interaction are poorly understood. Using yeast as a model, we show that the Insert B domain of the Dnm1 guanosine triphosphatase (a DRP) contains a novel motif required for association with the mitochondrial adaptor Mdv1. Mutation of this conserved motif specifically disrupted Dnm1-Mdv1 interactions, blocking Dnm1 recruitment and mitochondrial fission. Suppressor mutations in Mdv1 that restored Dnm1-Mdv1 interactions and fission identified potential protein-binding interfaces on the Mdv1 β-propeller domain. These results define the first known function for Insert B in DRP-adaptor interactions. Based on the variability of Insert B sequences and adaptor proteins, we propose that Insert B domains and mitochondrial adaptors have coevolved to meet the unique requirements for mitochondrial fission of different organisms.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism*
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Amino Acid Motifs
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Amino Acid Sequence
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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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Mitochondrial Membranes / metabolism*
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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, Molecular
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Molecular Sequence Data
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Mutation
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Saccharomyces cerevisiae / chemistry
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Saccharomyces cerevisiae / cytology*
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Sequence Alignment
Substances
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Adaptor Proteins, Signal Transducing
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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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GTP Phosphohydrolases
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DNM1 protein, S cerevisiae