Catalytic domain of the p120 Ras GAP binds to Rab5 and stimulates its GTPase activity

Kebin Liu, Guangpu Li

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Ras is a master GTPase switch controlling multiple signal transduction cascades in the regulation of cell proliferation and differentiation. Rab5 is a local GTPase switch that is localized on early endosomes and controls early endosome fusion. This study demonstrates that the catalytic domain of p120 GTPase-activating protein (GAP), a well known Ras GAP, is able to interact physically with Rab5 and stimulate its GTPase activity. This GAP activity toward Rab5, however, cannot be extended to other Rab GTPases such as Rab3, Rab4, and Rab6, indicating that it is not a generic GAP for the Rab family of GTPases that regulate intracellular membrane fusion during endocytosis and exocytosis. The findings indicate a level of structural similarity between Ras and Rab5 unexpected from their primary sequences. They also suggest a possible signal transduction regulation of the Rab5-dependent endosome fusion via the Ras GAP.

Original languageEnglish (US)
Pages (from-to)10087-10090
Number of pages4
JournalJournal of Biological Chemistry
Volume273
Issue number17
DOIs
StatePublished - Apr 24 1998
Externally publishedYes

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p120 GTPase Activating Protein
ras GTPase-Activating Proteins
Endosomes
GTP Phosphohydrolases
rab GTP-Binding Proteins
GTPase-Activating Proteins
Catalytic Domain
Signal transduction
Fusion reactions
Signal Transduction
Intracellular Membranes
Membrane Fusion
Switches
Exocytosis
Endocytosis
Cell Differentiation
Cell proliferation
Cell Proliferation
Membranes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Catalytic domain of the p120 Ras GAP binds to Rab5 and stimulates its GTPase activity. / Liu, Kebin; Li, Guangpu.

In: Journal of Biological Chemistry, Vol. 273, No. 17, 24.04.1998, p. 10087-10090.

Research output: Contribution to journalArticle

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