A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTpase Rab5

Kota Saito, Jun Murai, Hiroaki Kajiho, Kenji Kontani, Hiroshi Kurosu, Toshiaki Katada

研究成果: Article

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The small GTPase Rab family, which cycles between GTP-bound active and GDP-bound inactive states, plays an important role in membrane trafficking. Among them, Rab5 is involved in early endocytic pathway, and several Rab5-binding proteins have been identified as regulators or effectors to coordinate the docking and fusion processes of endocytic vesicles. We describe a novel binding protein exhibiting unique biochemical properties for Rab5. The Rab5-binding protein enhances GDP-GTP exchange reaction on Rab5 but preferentially interacts with its GTP-bound form. Gel filtration and immunoprecipitation analyses indicate that the Rab5-binding protein functions as a tetramer composed of anti-parallel linkage of two parallel dimers. These results suggest that the newly identified protein may function as an upstream activator and/or downstream effector for Rab5 in endocytic pathway. Possible roles of the quaternary structure have been discussed in terms of the Rab5-mediated signaling.

元の言語English
ページ(範囲)3412-3418
ページ数7
ジャーナルJournal of Biological Chemistry
277
発行部数5
DOI
出版物ステータスPublished - 2002 2 1
外部発表Yes

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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