| Modification Notes |
A critical step in signal transduction responses to stimulation of cell surface receptors by their ligands involves the accumulation of Ras proteins in their active GTP bound state. To reach their active GTP bound state, Ras proteins must first release bound GDP, a rate limiting step mediated by a guanine nucleotide releasing factor (GRF). The mammalian Ras p21 GRF protein has been designated Ras-GRF1 (also known as Ras-GRF1 p140). Ras-GRF1 accelerates release of GDP from H- and N-Ras p21 protein in vitro, but not from the related Ral A or Cdc42Hs GTP binding proteins. Of interest, a region mapping within the amino-terminal domain of Ras-GRF1 is similar to both the human breakpoint cluster protein Bcr and the Dbl proto-oncogene product, a guanine nucleotide-releasing factor for Cdc42Hs. Ras-GRF2 p135 has also been identified. Ras-GRF2 p135 is highly homologous to Ras-GRF1 and the two proteins appear to function in a similar manner. Human Ras-GRF1 is subject to phosphorylation at specific amino acid residues, including Ser 929. |