Replacement of Arg-386 with gly in dynamin 1 middle domain reduced GTPase activity and oligomer stability in the absence of lipids

Kiyofumi Takahashi, Masahiro Otomo, Noboru Yamaguchi, Hideki Nakashima, Hiroshi Miyoshi

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2195-2200
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume76
Issue number12
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • Disassembly
  • Dynamin
  • Endocytosis
  • Guanosine 5'-triphosphatase
  • Oligomer

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Analytical Chemistry
  • Organic Chemistry

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