Cited by 292Protein Kinase Regulation and GTPase SignalingCellular transport and secretionProtein Tyrosine Phosphatases

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Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.

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Hofer, F, Fields, S, Schneider, C, Martin, G S·1994·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.91.23.11089PMC PMC45172

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Abstract

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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Self-citation
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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
DOI: 10.1073/pnas.91.23.11089
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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Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.

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