Ral proteins, RalA and RalB, are members of the Ras family of small GTPases. Ral proteins are activated by guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP and facilitate the binding of Ral to its various downstream effector proteins. GTPase-activating proteins (GAPs) stimulate the hydrolysis of GTP to GDP, which inactivates Ral.
The discovery that many tumors contained a transforming Ras allele (HRAS, KRAS and NRAS) in the 1980s spurred interest in identifying new members of the Ras family. In 1986, Pierre Chardin and Armand Tavitian synthesized a 20-mer oligonucleotide probe corresponding to a conserved region of Ras proteins to identify novel Ras genes by screening a simian B-cell line cDNA library (Chardin and Tavitian 1986). The screen resulted in the discovery of an open reading frame that shared a high degree of homology with the three Ras genes and was consequently named Ral (Ras-like). The...
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