Regulators of small GTPases.

Y. Takai, K. Kaibuchi, A. Kikuchi, T. Sasaki, H. Shirataki

Research output: Contribution to journalReview articlepeer-review

27 Citations (Scopus)

Abstract

Small GTPases are converted from the GDP-bound inactive form to the GTP-bound active form by a GDP/GTP exchange reaction which is regulated by GDP/GTP exchange proteins (GEPs). We have found both stimulatory and inhibitory GEPs, which we have named GDP dissociation stimulators (GDSs) and GDP dissociation inhibitors (GDIs) respectively. We have isolated Smg GDS, Rho GDI and Rab GDI, cloned them, and determined their primary structures. These GEPs are active on a group of small GTPases: Smg GDS on at least K-Ras, Rap1/Smg21, Rho and Rac; Rho GDI on at least Rho, Rac and Cdc42; Rab GDI on most of the Rab family members. These GEPs have an additional function, regulating the translocation of their substrate small GTPases between the membrane and the cytosol. The GEPs interact only with the post-translationally modified form of their substrate small GTPases.

Original languageEnglish
Pages (from-to)128-138; discussion 138-146
JournalCiba Foundation symposium
Volume176
Publication statusPublished - 1993
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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