“Atypical Rho Family Members“

Ana Barbara Damasceno Borda D'Agua; Elvira Infante; Philippe Jean Louis Riou; Virginia Tajadura-Ortega; Anne Ridley

doi:10.1007/978-3-7091-1806-1_15

“Atypical Rho Family Members“

Ana Barbara Damasceno Borda D'Agua, Elvira Infante, Philippe Jean Louis Riou, Virginia Tajadura-Ortega, Anne Ridley

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

1 Citation (Scopus)

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.

Original language	English
Title of host publication	Ras Superfamily Small G Proteins: Biology and Mechanisms 1
Editors	Alfred Wittinghofer
Publisher	Springer
Pages	341-361
Volume	1
Edition	May 2014
ISBN (Electronic)	9783709118061
DOIs	https://doi.org/10.1007/978-3-7091-1806-1_15
Publication status	Published - 2014

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title = "“Atypical Rho Family Members“",

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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T1 - “Atypical Rho Family Members“

AU - Borda D'Agua, Ana Barbara Damasceno

AU - Infante, Elvira

AU - Riou, Philippe Jean Louis

AU - Tajadura-Ortega, Virginia

AU - Ridley, Anne

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

U2 - 10.1007/978-3-7091-1806-1_15

DO - 10.1007/978-3-7091-1806-1_15

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BT - Ras Superfamily Small G Proteins: Biology and Mechanisms 1

A2 - Wittinghofer, Alfred

PB - Springer

ER -

“Atypical Rho Family Members“

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