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*

*この研究の対応する著者

研究成果: Article査読

2 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)2195-2200
ページ数6
ジャーナルBioscience, Biotechnology and Biochemistry
76
12
DOI
出版ステータスPublished - 2012
外部発表はい

ASJC Scopus subject areas

  • バイオテクノロジー
  • 生化学
  • 分子生物学
  • 応用微生物学とバイオテクノロジー
  • 分析化学
  • 有機化学

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