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Science 16 November 1990: Vol. 250. no. 4983, pp. 982 - 985 DOI: 10.1126/science.2237442
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Articles
Science, Vol 250, Issue 4983, 982-985
Copyright © 1990 by American Association for the Advancement of Science
A cytoplasmic protein inhibits the GTPase activity of H-Ras in a phospholipid-dependent manner
MH Tsai,
CL Yu,
and
DW Stacey
Department of Molecular Biology, Cleveland Clinic Foundation 44195.
A cytoplasmic protein has been identified that inhibits the guanosine triphosphatase (GTPase) activity of bacterially synthesized, cellular H-Ras protein. This GTPase inhibiting protein is able to counteract the activity of GTPase activating protein (GAP), which has been postulated to function as a negative regulator of Ras activity. The potential biological importance of the GTPase inhibiting protein is further supported by its interaction with lipids. Phospholipids produced in cells as a consequence of mitogenic stimulation increase the activity of the GTPase inhibiting protein, as well as inhibit the activity of GAP. The interaction of such lipids with each of these two regulatory proteins would, therefore, tend to increase the biological activity of Ras and stimulate cell proliferation.
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