Tsai M H, Yu C L, Stacey D W
Department of Molecular Biology, Cleveland Clinic Foundation 44195.
Science. 1990 Nov 16;250(4983):982-5. doi: 10.1126/science.2237442.
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.
已鉴定出一种细胞质蛋白,它可抑制细菌合成的细胞H-Ras蛋白的鸟苷三磷酸酶(GTPase)活性。这种GTPase抑制蛋白能够抵消GTPase激活蛋白(GAP)的活性,GAP被认为是Ras活性的负调节因子。GTPase抑制蛋白与脂质的相互作用进一步证明了其潜在的生物学重要性。有丝分裂刺激后细胞中产生的磷脂会增加GTPase抑制蛋白的活性,并抑制GAP的活性。因此,这些脂质与这两种调节蛋白的相互作用往往会增加Ras的生物学活性并刺激细胞增殖。