Studies of RAS Function in the Yeast Saccharomyces cerevisiae
- M. Wigler*,
- J. Field*,
- S. Powers†,
- D. Broek‡,
- T. Toda§,
- S. Cameron**,
- J. Nikawa††,
- T. Michaeli*,
- J. Colicelli*, and
- K. Ferguson*
- *Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; ††Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854; ‡Kenneth Norris, Jr., Cancer Research Hospital and Research Institute, Los Angeles, California 90033; §Department of Biophysics, Faculty of Science, Kyoto University, Kyoto 606, Japan; **Harvard Medical School/Massachusetts Institute of Technology, Program in Health Science & Technology, Cambridge, Massachusetts 02115; ††Department of Biochemistry, Gunma University, School of Medicine, Maebashi, Gunma 371, Japan
This extract was created in the absence of an abstract.
Excerpt
The three mammalian RAS genes, Ha-ras, Ki-ras, and N-ras, are capable of the malignant transformation of cultured animal cells (Barbacid 1987). Mutations in these genes have been linked to a large number of human cancers (Barbacid 1987). These genes encode closely related proteins that bind guanine nucleotides (Scolnick et al. 1979; Shih et al. 1980; Ellis et al. 1981) and are localized to the inner surface of the plasma membrane (Willingham et al. 1980; Papageorge et al, 1982). Normal RAS proteins also slowly hydrolyze GTP (Gibbs et al. 1984; McGrath et al. 1984; Sweet et al. 1984). These properties are similar to those of the G proteins, which has led to the widespread expectation that RAS proteins, like G proteins, are involved in the transduction of membrane signals that are linked to cellular proliferation or differentiation. Many of the mutations that activate the RAS genes result in the production of...
