This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Elam, C. Articles by Clark, G. J. Search for Related Content PubMed PubMed Citation Articles by Elam, C. Articles by Clark, G. J.

RRP22 Is a Farnesylated, Nucleolar, Ras-Related Protein with Tumor Suppressor Potential

¹ Department of Cell and Cancer Biology, National Cancer Institute, Rockville, Maryland; ² Section of Medical and Molecular Genetics, Division of Reproductive and Child Health, University of Birmingham, Birmingham, United Kingdom; and ³ Department of Neurosurgery, Universitätsklinikum Carl Gustav Carus, Technische Universität Dresden, Dresden, Germany

Requests for reprints: Geoffrey J. Clark, Department of Cell and Cancer Biology, National Cancer Institute-NIH, Room 307, 9610 Medical Center Drive, Rockville, MD 20820-3300. Phone: 301-594-7288; Fax: 301-402-4422; E-mail: gclark{at}mail.nih.gov.

Ras proteins are members of a superfamily of related small GTPases. Some members, such as Ras, are oncogenic. However, other members seem to serve as tumor suppressors, such as Rig and Noey2. We now identify and characterize a novel member of the Ras superfamily, RRP22. Like Ras, RRP22 can be posttranslationally modified by farnesyl. Unlike Ras, RRP22 inhibits cell growth and promotes caspase-independent cell death. Examination of human tumor cells shows that RRP22 is frequently down-regulated due to promoter methylation. Moreover, reexpression of RRP22 in an RRP22-negative neural tumor cell line impairs its growth in soft agar. Unusually for a Ras-related protein, RRP22 localizes to the nucleolus in a GTP-dependent manner, suggesting a novel mechanism of action. Thus, we identify a new member of the Ras superfamily that can serve as a potential tumor suppressor.

This article has been cited by other articles:

				A. Galichet and W. Gruissem Developmentally Controlled Farnesylation Modulates AtNAP1;1 Function in Cell Proliferation and Cell Expansion during Arabidopsis Leaf Development Plant Physiology, December 1, 2006; 142(4): 1412 - 1426. [Abstract] [Full Text] [PDF]

				A. D. Basso, P. Kirschmeier, and W. R. Bishop Thematic review series: Lipid Posttranslational Modifications. Farnesyl transferase inhibitors J. Lipid Res., January 1, 2006; 47(1): 15 - 31. [Abstract] [Full Text] [PDF]

				E. David, S.-Y. Sun, E. K. Waller, J. Chen, F. R. Khuri, and S. Lonial The combination of the farnesyl transferase inhibitor lonafarnib and the proteasome inhibitor bortezomib induces synergistic apoptosis in human myeloma cells that is associated with down-regulation of p-AKT Blood, December 15, 2005; 106(13): 4322 - 4329. [Abstract] [Full Text] [PDF]