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“Atypical Rho Family Members“

Research output: Chapter in Book/Report/Conference proceedingChapter

Original languageEnglish
Title of host publicationRas Superfamily Small G Proteins: Biology and Mechanisms 1
EditorsAlfred Wittinghofer
PublisherSpringer
Pages341-361
Volume1
EditionMay 2014
ISBN (Electronic)9783709118061
DOIs
Published2014

King's Authors

Abstract

Of the 20 Rho GTP-binding proteins in humans, 8 have atypical properties, which are also unusual within the Ras superfamily. These atypical proteins fall into four subfamilies: RhoU/RhoV, Rnd1/Rnd2/Rnd3, RhoH and RhoBTB1/RhoBTB2. These proteins are known or predicted to be predominantly GTP-bound in cells, because of changes in their ability to exchange GDP for GTP or to hydrolyse GTP. Apart from RhoH, they also have N-terminal and C-terminal extensions that give them unique interacting partners and functions. For example, RhoU can bind SH3 domain-containing proteins, Rnd proteins can bind to 14-3-3 proteins, and RhoBTB proteins can interact via their BTB domains with cullin-3, which is involved in proteasomal degradation. The proteins have been implicated in diverse functions, including cell adhesion and migration, vesicle trafficking and cell proliferation.

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