Replacement of Arg-386 with Gly in Dynamin 1 Middle Domain Reduced GTPase Activity and Oligomer Stability in the Absence of Lipids

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  • TAKAHASHI Kiyofumi
    Department of Neuropsychiatry, St. Marianna University School of Medicine
  • OTOMO Masahiro
    Department of Neuropsychiatry, St. Marianna University School of Medicine
  • YAMAGUCHI Noboru
    Department of Neuropsychiatry, St. Marianna University School of Medicine
  • NAKASHIMA Hideki
    Department of Microbiology, St. Marianna University School of Medicine
  • MIYOSHI Hiroshi
    Department of Microbiology, St. Marianna University School of Medicine

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Abstract

Dynamin plays an important role in membrane fission during endocytosis, and its middle domain is involved in the formation of functional oligomers. In this study, we found that replacement of Arg-386 with Gly in the middle domain region of dynamin 1 did not affect the intermolecular interactions of dynamin 1 in the presence of phosphatidylserine-liposomes. But, unexpectedly, this variant showed lower guanosine 5′-triphosphatase activity in the absence of phosphatidylserine-liposomes and enhanced monomer formation from oligomers. Our results indicate that GTPase activity in the absence of lipids is important in the dissociation of oligomer complexes, i.e., reduced basal dynamin 1 GTPase activity is associated with instability of dynamin oligomers.

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