This Article 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 Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hoshino, M Articles by Hattori, S Search for Related Content PubMed PubMed Citation Articles by Hoshino, M Articles by Hattori, S

 Previous Article  |  Next Article 

Mol Cell Biol. 1988 October; 8(10): 4169-4173

Characterization of a factor that stimulates hydrolysis of GTP bound to ras gene product p21 (GTPase-activating protein) and correlation of its activity to cell density.

Department of Pure and Applied Sciences, College of Arts and Sciences, University of Tokyo, Japan.

ABSTRACT

The postmicrosomal fraction of the extract from NIH 3T3 and BALB/c 3T3 cells stimulated the hydrolysis of GTP bound to H-ras gene product p21 by severalfold. The stimulation was observed with normal p21 but not with p21 with valine as the 12th residue. This specificity is similar to that of GTPase-activating protein (GAP) for N-ras p21 described by M. Trahey and F. McCormick (Science 238:542-545, 1987). Consistent with this specificity, analysis of p21-bound nucleotides in living cells revealed that almost all normal p21 bound GDP, whereas oncogenic mutant p21s bound both GTP and GDP. Similar activity was also found in various mouse tissues, with brain tissue showing the highest specific activity. When cell extracts were prepared from cultured cells, there was a linear relationship between GAP activity and cell density. These results suggest the factor is involved in the regulation of cell proliferation.

This article has been cited by other articles:

• Yunoue, S., Tokuo, H., Fukunaga, K., Feng, L., Ozawa, T., Nishi, T., Kikuchi, A., Hattori, S., Kuratsu, J., Saya, H., Araki, N. (2003). Neurofibromatosis Type I Tumor Suppressor Neurofibromin Regulates Neuronal Differentiation via Its GTPase-activating Protein Function toward Ras. J. Biol. Chem. 278: 26958-26969 [Abstract] [Full Text]  
• Koehler, J. A., Moran, M. F. (2001). Regulation of Extracellular Signal-regulated Kinase Activity by p120 RasGAP Does Not Involve Its Pleckstrin Homology or Calcium-dependent Lipid Binding Domains but Does Require These Domains to Regulate Cell Proliferation. Cell Growth Differ. 12: 551-561 [Abstract] [Full Text]  
• Ghai, J., Ostrow, R. S., Tolar, J., McGlennen, R. C., Lemke, T. D., Tobolt, D., Liu, Z., Faras, A. J. (1996). The E5 gene product of rhesus papillomavirus is an activator of endogenous Ras and phosphatidylinositol-3'-kinase in NIH 3T3 cells. Proc. Natl. Acad. Sci. USA 93: 12879-12884 [Abstract] [Full Text]  
• Zhang, K, Papageorge, A., Lowy, D. (1992). Mechanistic aspects of signaling through Ras in NIH 3T3 cells. Science 257: 671-674 [Abstract]  
• Buss, J., Solski, P., Schaeffer, J., MacDonald, M., Der, C. (1989). Activation of the cellular proto-oncogene product p21Ras by addition of a myristylation signal. Science 243: 1600-1603 [Abstract]