A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function

Hisanori Horiuchi, Roger Lippé, Heidi M. McBride, Mariantonietta Rubino, Philip Woodman, Harald Stenmark, Vladimir Rybin, Matthias Wilm, Keith Ashman, Matthias Mann, Marino Zerial

研究成果: Article査読

482 被引用数 (Scopus)

抄録

The small GTPase Rab5 plays an essential role in endocytic traffic. Rab GDP dissociation inhibitor delivers Rab5 to the membrane, where a nucleotide exchange activity allows recruitment of an effector protein, Rab-aptin-5. Here we uncovered a novel 60 kDa Rab5-binding protein, Rabex-5. Rabex-5 forms a tight physical complex with Rabaptin-5, and this complex is essential for endocytic membrane fusion. Sequencing of mammalian Rabex-5 by nanoelectrospray mass spectrometry and cloning revealed striking homology to Vps9p, a yeast protein implicated in endocytic traffic. Rabex-5 displays GDP/GTP exchange activity on Rab5 upon delivery of the GTPase to the membrane. This demonstrates that a soluble exchange factor coupled to a Rab effector translocates from cytosol to the membrane, where the complex stabilizes the GTPase in the active state.

本文言語English
ページ(範囲)1149-1159
ページ数11
ジャーナルCell
90
6
DOI
出版ステータスPublished - 1997 9月 19
外部発表はい

ASJC Scopus subject areas

  • 生化学、遺伝学、分子生物学(全般)

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