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Science 31 July 1992:
Vol. 257. no. 5070, pp. 671 - 674
DOI: 10.1126/science.1496380
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Articles

Science, Vol 257, Issue 5070, 671-674
Copyright © 1992 by American Association for the Advancement of Science

articles

Mechanistic aspects of signaling through Ras in NIH 3T3 cells

K Zhang, AG Papageorge, and DR Lowy

Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, MD 20892.

Serum and growth factors can increase the proportion of Ras in the active guanosine triphosphate (GTP)-bound form. Growth factors might stimulate guanine nucleotide exchange or decrease the activity of the guanosine triphosphatase-activating proteins GAP and neurofibromin (NF1). In NIH 3T3 cells that overexpress the mutant Ras protein His116, which releases bound guanine nucleotide at a constitutively high rate and retains sensitivity to GAP and NF1, the proportion of GTP bound to the His116 protein was not altered by serum or platelet-derived growth factor. However, these mitogens increased the proportion of Ras in the GTP-bound form in cells that overexpressed control Ras proteins with a normal intrinsic rate of guanine nucleotide release. The amount of GTP-bound His116 or control Ras proteins was higher in cells at low density than in cells at high density, which have more GAP-like activity. The lower proportion of GTP-bound Ras in NIH 3T3 cells at high density may result from increased GAP-like activity. By contrast, serum and platelet-derived growth factors appear to stimulate guanine nucleotide exchange.


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