Influence of p21ras on Phosphatidylinositol Turnover

  1. J. Downward and
  2. R.A. Weinberg
  1. Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142

This extract was created in the absence of an abstract.

Excerpt

The ras gene family is of great importance in human malignancy: Point mutation of these genes at a number of positions activates their oncogenic potential, resulting in mutant proteins capable of transforming cells even when expressed at relatively low levels. The mechanisms by which the activated ras-encoded 21,000-molecular-weight proteins transform cells and the roles of their normal counterparts have been the subjects of intense speculation. ras proteins bind and hydrolyze guanosine triphosphate; the hydrolytic activity is impaired in the transforming protein as compared to normal p21 (McGrath et al. 1984; Sweet et al. 1984). Localized sequence homologies exist between ras proteins and the family of mammalian GTP-binding proteins termed “G proteins,” which couple a wide variety of cell-surface receptors to intracellular enzyme systems (Lochrie et al. 1985; Medynski et al. 1985; Tanabe et al. 1985; Yatsunami et al. 1985). Both sets of proteins are also known to be peripherally associated...

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