The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.
Open accessAbstract
The yeast two-hybrid system was used to identify proteins that interact with Ras. The H-Ras protein was found to interact with a guanine nucleotide dissociation stimulator (GDS) that has been previously shown to regulate guanine nucleotide exchange on another member of the Ras protein family, Ral. The interaction is mediated by the C-terminal, noncatalytic segment of the RalGDS and can be detected both in vivo, using the two-hybrid system, and in vitro, with purified recombinant proteins. The interaction of the RalGDS C-terminal segment with Ras is specific, dependent on activation of Ras by GTP, and blocked by a mutation that affects Ras effector function. These characteristics are similar to those previously demonstrated for the interaction between Ras and its putative effector, Raf, suggesting that the RalGDS may also be a Ras effector. Consistent with this idea, the RalGDS was found to inhibit the binding of Raf to Ras.
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“Ral can be activated either by Ras indirectly via a Ral-GEF (Guanine nucleotide Exchange Factor) or by Ca 2 þ /calmodulin binding (Hofer et al, 1994(Hofer et al, , 1998;;Kikuchi et al, 1994;Wolthuis et al, 1998;Wang and Roufogalis, 1999;Wolthuis and Bos, 1999;Harvey et al, 2008)”
From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Hofer et al, 1994
In the citing paper
“KRAS activation leads to downstream signaling of three major pathways: the MAP kinase pathway, PI3K-AKT-mTOR pathway, and the tumour invasion and metastasis-inducing protein 1 (TIAM1-RAC) and RAS-related protein (RAL) pathways (Fig. 3).”
From Drugging KRAS: Current perspectives and state-of-art review (2022) · cites this paper as [39]
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Metadata
- Authors
- Hofer, F., Fields, S., Schneider, C., & Martin, G. S.
- Affiliations
- University of California, Berkeley (US)
- ORCID
- Fields, S
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1994-11-08
- Volume
- 91
- Issue
- 23
- Pages
- 11089-11093
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC45172
- OpenAlex
- W2012189464
- Cited by
- 287
- References
- 30
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 5 · 2023: 6 · 2022: 13 · 2021: 4 · 2020: 9 · 2019: 4 · 2018: 5 · 2017: 8 · 2016: 8 · 2015: 6 · 2014: 3 · 2013: 9
- FWCI
- 9.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA17542, P01CA028146, CA-28146)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- Ras, RalGDS, protein-protein interaction, Ras effectors, guanine nucleotide exchange, Ras activation, Raf, Ras family
- MeSH terms
- Amino Acid Sequence, Binding Sites, Binding, Competitive, Humans, Molecular Sequence Data, Protein Binding, Proto-Oncogene Proteins, Structure-Activity Relationship, Proto-Oncogene Proteins p21(ras), Mutagenesis, Site-Directed, Sequence Alignment, Protein Serine-Threonine Kinases, Sequence Homology, Amino Acid, GTP-Binding Proteins, Proto-Oncogene Proteins c-raf, ral GTP-Binding Proteins, In Vitro Techniques
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