ArticleThe EMBO journal1992
RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 56 citations in OpenAlex.
- Targeting KRAS mutations: orchestrating cancer evolution and therapeutic challenges.Signal transduction and targeted therapy · 2025Review
- 40 Years of RAS-A Historic Overview.Genes · 2021Review
- A novel HRAS substitution (c.266C>G; p.S89C) resulting in decreased downstream signaling suggests a new dimension of RAS pathway dysregulation in human development.American journal of medical genetics. Part A · 2012Article
- Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner.Molecular and cellular biology · 1998Article
- A glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1.The EMBO journal · 1998Article
- Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G.Molecular and cellular biology · 1995Article
- Aberrant function of the Ras-related protein TC21/R-Ras2 triggers malignant transformation.Molecular and cellular biology · 1994Article
- Distinct structural elements of rab5 define its functional specificity.The EMBO journal · 1994Article
- Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors.Molecular and cellular biology · 1994Article
- Identification of residues of the H-ras protein critical for functional interaction with guanine nucleotide exchange factors.Molecular and cellular biology · 1994Article
- Residues crucial for Ras interaction with GDP-GTP exchangers.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase.The EMBO journal · 1993Article
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10 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We have previously shown that a conserved glycine at position 82 of the yeast RAS2 protein is involved in the conversion of RAS proteins from the GDP- to the GTP-bound form. We have now investigated the role of glycine 82 and neighbouring amino acids of the distal switch II region in the physiological mechanism of activation of RAS. We have introduced single and double amino acid substitutions at positions 80-83 of the RAS2 gene, and we have investigated the interaction of the corresponding proteins with a yeast GDP dissociation stimulator (SDC25 C-domain). Using purified RAS proteins, we have found that the SDC25-stimulated conversion of RAS from the GDP-bound inactive state to the GTP-bound active state was severely impaired by amino acid substitutions at positions 80-81. However, the rate and the extent of conversion from the GDP- to the GTP-bound form in the absence of dissociation factor was unaffected. The insensitivity of the mutated proteins to the dissociation factor in vitro was paralleled by an inhibitory effect on growth in vivo. The mutations did not significantly affect the interaction of RAS with adenylyl cyclase. These findings point to residues 80-82 as important determinants of the response of RAS to GDP dissociation factors. This suggests a molecular model for the enhancement of nucleotide release from RAS by such factors.
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