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Sci. STKE, 21 August 2001
Vol. 2001, Issue 96, p. pe2
[DOI: 10.1126/stke.2001.96.pe2]

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Ras Isoform-Specific Signaling: Location, Location, Location

Alan Wolfman

The author is at the Department of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA. E-mail: wolfmaa{at}ccf.org

Abstract: The proteins that compose the Ras family of small guanosine triphosphatases share a remarkably high degree of sequence similarity, yet recent evidence indicates that they may have unique biological properties. How is it that similar proteins carry out different jobs in the cell? Wolfman addresses this question by surveying recent reports that indicate that different biological roles may be born out of distinct subcellular localizations of the Ras proteins. It appears that the small differences in their amino acid sequences and their different posttranslational modifications may be all that is necessary to direct various Ras proteins to different sites.

Citation: A. Wolfman, Ras Isoform-Specific Signaling: Location, Location, Location. Sci. STKE 2001, pe2 (2001).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Differences in the Regulation of K-Ras and H-Ras Isoforms by Monoubiquitination.
R. Baker, E. M. Wilkerson, K. Sumita, D. G. Isom, A. T. Sasaki, H. G. Dohlman, and S. L. Campbell (2013)
J. Biol. Chem. 288, 36856-36862
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