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A novel motif in the yeast mitochondrial dynamin Dnm1 is essential for adaptor binding and membrane recruitment.

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.

Pubmed ID: 23148233


  • Bui HT
  • Karren MA
  • Bhar D
  • Shaw JM


The Journal of cell biology

Publication Data

November 12, 2012

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM53466
  • Agency: NIGMS NIH HHS, Id: GM84970
  • Agency: NIGMS NIH HHS, Id: R01 GM053466

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs
  • Amino Acid Sequence
  • GTP Phosphohydrolases
  • Mitochondrial Membranes
  • Mitochondrial Proteins
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment