Human RAS Superfamily Proteins and Related GTPases

John Colicelli^*

Department of Biological Chemistry and Molecular Biology Institute, University of California Los Angeles, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.

Gloss: Proteins that bind and hydrolyze GTP (guanosine triphosphate), known as GTPases, are pervasive mediators of intracellular signal transduction. Among the first human GTPases studied were the RAS proteins, which are often found in mutated, hyperactive forms in cancer cells. Over the past 25 years, a family of RAS-related proteins has been identified. This review considers recent progress in understanding the biochemical properties and biological function of RAS family proteins. Analysis of the human genome was used to identify novel members of this family. In addition, comparisons with the completed genomes of fly and worm revealed new insights into evolution and structural conservation, with implications for predicting function. An overview of the full complement of human RAS superfamily proteins, and how they fit within a larger group of human GTPases, is presented.

*To whom correspondence should be addressed. E-mail: colicelli{at}mednet.ucla.edu

The editors suggest the following Related Resources on Science sites:

In Science Signaling

EDITORS' CHOICE
MITOSIS
Small GTPase Controls Chromosome Segregation

(21 September 2004)
Sci. STKE 2004 (251), tw337. [DOI: 10.1126/stke.2512004tw337]
 |  Abstract »

REVIEWS
Ypt/Rab GTPases: Regulators of Protein Trafficking

Nava Segev (18 September 2001)
Sci. STKE 2001 (100), re11. [DOI: 10.1126/stke.2001.100.re11]
 |  Gloss »  |  Abstract »  |  Full Text »  |  PDF »

REVIEWS
Molecular Aspects of the Cellular Activities of ADP-Ribosylation Factors

Paul A. Randazzo, Zhongzhen Nie, Koichi Miura, and Victor W. Hsu (21 November 2000)
Sci. STKE 2000 (59), re1. [DOI: 10.1126/stke.2000.59.re1]
 |  Gloss »  |  Abstract »  |  Full Text »  |  PDF »