Post-translational Modifications of Ras and Ral Are Important for the Action of Ral GDP Dissociation Stimulator
Open accessAbstract
Ral GDP dissociation stimulator (RalGDS) is a GDP/GTP exchange protein of Ral and a new effector protein of Ras. Therefore, there may be a new signaling pathway from Ras to Ral. In this paper, we examined the roles of the post-translational modifications of Ras and Ral on this new signal transduction pathway. The post-translationally modified form of Ras bound to RalGDS more effectively than the unmodified form. The modification of Ras was required to regulate the distribution of RalGDS between the cytosol and membrane fractions in COS cells. The post-translational modification of Ral enhanced the activities of RalGDS to stimulate the dissociation of GDP from and the binding of GTP to Ral. Furthermore, the modified form of Ral bound to Ral-binding protein 1 (RalBP1), a putative effector protein of Ral, more effectively than the unmodified form. Taken together with the observations that Ras and Ral are localized to the membranes, these results suggest that the post-translational modifications of Ras and Ral play a role for transmitting the signal effectively on the membranes in the signal transduction pathway of Ras/RalGDS/Ral/RalBP1.
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Overexpression of constitutively active RalAG23V or RalBG23V, which do not bind these compounds, mitigated inhibition of H2122 and H358 cell growth by these compounds.
“Lastly, overexpression of a constitutively active (GTP-form22) RalAG23V or RalBG23V, which do not bind these compounds (Extended Data Fig. 3d, 4b), mitigated inhibition of H2122 and H358 cell growth by these compounds (Fig. 3g–j, Extended Data Fig. 6f).”
From Discovery and characterization of small molecules that target the GTPase Ral (2014) · cites this paper as [22]
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Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.
Hofer, F., Fields, S., Schneider, C., & Martin, G. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11089 · Cited by 287 · see citing works
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Discovery and characterization of small molecules that target the GTPase Ral
Yan, C., Liu, D., Li, L., Wempe, M. F., Guin, S., Khanna, M., Meier, J., Hoffman, B., Owens, C., Wysoczynski, C. L., et al. (2014) · Nature · doi:10.1038/nature13713 · Cited by 150 · see citing works
- Authors
- Hinoi, T., Kishida, S., Koyama, S., Ikeda, M., Matsuura, Y., & Kikuchi, A.
- Affiliations
- Hiroshima University (JP)
- Corresponding author
- Kikuchi, Akira
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-08
- Volume
- 271
- Issue
- 33
- Pages
- 19710-19716
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1983011848
- Cited by
- 38
- References
- 1
- Citations by year
- 2026: 1 · 2021: 1 · 2020: 1 · 2018: 1 · 2014: 2 · 2013: 1 · 2012: 1
- FWCI
- 2.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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 › Sphingolipid Metabolism and Signaling
- Keywords
- Ras, Ral, RALBP1, post-translational modification, GDP/GTP exchange, signal transduction, membrane localization
- MeSH terms
- Amino Acid Sequence, Animals, Carrier Proteins, Cell Compartmentation, Cell Membrane, Chlorocebus aethiops, Fungal Proteins, Molecular Sequence Data, Protein Binding, Protein Processing, Post-Translational, Recombinant Proteins, Structure-Activity Relationship, Signal Transduction, Proto-Oncogene Proteins p21(ras), Point Mutation, GTP-Binding Proteins, rap GTP-Binding Proteins, GTPase-Activating Proteins, ral GTP-Binding Proteins, ral Guanine Nucleotide Exchange Factor, Macromolecular Substances
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