Cited by 1,211Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesCellular transport and secretion

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A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants

Trahey, Meg, McCormick, Frank·1987·Science

DOI 10.1126/science.2821624

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Abstract

The role of guanine nucleotides in ras p21 function was determined by using the ability of p21 protein to induce maturation of Xenopus oocytes as a quantitative assay for biological activity. Two oncogenic mutant human N- ras p21 proteins, Asp12 and Val12, actively induced maturation, whereas normal Gly12 p21 was relatively inactive in this assay. Both mutant proteins were found to be associated with guanosine triphosphate (GTP) in vivo. In contrast, Gly12 p21 was predominantly guanosine diphosphate (GDP)-bound because of a dramatic stimulation of Gly12 p21-associated guanosine triphosphatase (GTPase) activity. A cytoplasmic protein was shown to be responsible for this increase in activity. This protein stimulated GTP hydrolysis by purified Gly12 p21 more than 200-fold in vitro, but had no effect on Asp12 or Val12 mutants. A similar factor could be detected in extracts from mammalian cells. It thus appears that, in Xenopus oocytes, this protein maintains normal p21 in a biologically inactive, GDP-bound state through its effect on GTPase activity. Furthermore, it appears that the major effect of position 12 mutations is to prevent this protein from stimulating p21 GTPase activity, thereby allowing these mutants to remain in the active GTP-bound state.

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Monoclonal antibodies to the p21 products of the transforming gene of Harvey murine sarcoma virus and of the cellular ras gene family
Furth, M. E., Davis, L. J., Fleurdelys, B. E., & Scolnick, E. M. (1982) · Journal of Virology · doi:10.1128/jvi.43.1.294-304.1982 · Cited by 800
Comparative biochemical properties of normal and activated human ras p21 protein
McGrath, J. P., Capon, D. J., Goeddel, D. V., & Levinson, A. D. (1984) · Nature · doi:10.1038/310644a0 · Cited by 699
Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins
JURNAK, F. A. (1985) · Science · doi:10.1126/science.3898365 · Cited by 621
Intrinsic GTPase activity distinguishes normal and oncogenic ras p21 molecules.
Gibbs, W. W., Sigal, I. S., Poe, M., & Scolnick, E. M. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.18.5704 · Cited by 580
Biological and biochemical properties of human rasH genes mutated at codon 61
Der, C. J., Finkel, T., & Cooper, G. M. (1986) · Cell · doi:10.1016/0092-8674(86)90495-2 · Cited by 536
The product of ras is a GTPase and the T24 oncogenic mutant is deficient in this activity
Sweet, R. W., Yokoyama, S., Kamata, T., Feramisco, J. R., Rosenberg, M. J., & Gross, M. S. (1984) · Nature · doi:10.1038/311273a0 · Cited by 532
RAS proteins can induce meiosis in xenopus oocytes
Birchmeier, C., Broek, D., & Wigler, M. H. (1985) · Cell · doi:10.1016/0092-8674(85)90233-8 · Cited by 342
Changes in protein phosphorylation accompanying maturation of Xenopus laevis oocytes
Maller, J. L., Wu, M. W., & Gerhart, J. C. (1977) · Developmental Biology · doi:10.1016/0012-1606(77)90093-8 · Cited by 276
Partial purification and characterization of the maturation-promoting factor from eggs of Xenopus laevis
Wu, M., & Gerhart, J. C. (1980) · Developmental Biology · doi:10.1016/0012-1606(80)90131-1 · Cited by 245

Show all 23 references

Research works printed but not linked: 2

Gibbs, J. B., Proceedings of the National Academy of Sciences of the United States of America 81: 5704 (1984).
Manne, V., Proceedings of the National Academy of Sciences of the United States of America 81: 6953 (1984).

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A structure and some function
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Méndez‐Sánchez, N., Vásquez‐Fernández, F., Zamora‐Valdés, D., & Uribe, M. (2008) · Annals of Hepatology · doi:10.1016/s1665-2681(19)31886-1 · Cited by 37
Molecular dynamics simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: flexibility, possible hinges, and levers of the conformational transition
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Hydrolysis of GTP by the α‐chain of Gs and other GTP binding proteins
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Heterogeneous Amino Acids in Ras and Rap1A Specifying Sensitivity to GAP Proteins
Zhang, K., Papageorge, A. G., Martin, P., Vass, W. C., Oláh, Z., Polakis, P. G., McCormick, F. P., & Lowy, D. R. (1991) · Science · doi:10.1126/science.1749934 · Cited by 37
Self-citation
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Horiuchi, H., Kaibuchi, K., Kawamura, M., Matsuura, Y., Suzuki, N., Kuroda, Y., Kataoka, T., & Takai, Y. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.10.4515 · Cited by 37
Purification and characterization from bovine brain membranes of a GTP-binding protein with a Mr of 21,000, ADP-ribosylated by an ADP-ribosyltransferase contaminated in botulinum toxin type C1 4- Identification as the rhoA gene product
Hoshijima, M., Kondo, J., Kikuchi, A., Yamamoto, K., & Takai, Y. (1990) · Molecular Brain Research · doi:10.1016/0169-328x(90)90067-n · Cited by 37
[35] Ypt proteins in yeast
Wagner, P., Hengst, L., & Gallwitz, D. (1992) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(92)19037-7 · Cited by 37
YsxC, an essential protein in Staphylococcus aureus crucial for ribosome assembly/stability
Cooper, E. L., Garcı́a-Lara, J., & Foster, S. J. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-266 · Cited by 36
The SpoIIAA protein of Bacillus subtilis has GTP-binding properties
Najafi, S. M. A., Harris, D. A., & Yudkin, M. D. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.22.6632-6634.1996 · Cited by 36
Mutations in cell division cycle genes CDC36 and CDC39 activate the Saccharomyces cerevisiae mating pheromone response pathway.
Lopes, M. D. B., Ho, J., & Reed, S. I. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.6.2966 · Cited by 36
RAS GENES AND ACUTE MYELOID LEUKAEMIA
Toksoz, D., Farr, C. J., & Marshall, C. J. (1989) · British Journal of Haematology · doi:10.1111/j.1365-2141.1989.tb06265.x · Cited by 35
Molecular Cloning and Characterization of a Novel Type of Regulatory Protein (GDI) for smg p25A, a ras p21-Like GTP-Binding Protein
Matsui, Y., Kikuchi, A., Araki, S., Hata, Y., Kondo, J., Teranishi, Y., & Takai, Y. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4116-4122.1990 · Cited by 36
Acute presentation of a neurogenic sarcoma in a patient with neurofibromatosis type 1: a pathological and molecular explanation
Feldkamp, M. M., Lau, N. C., Provias, J., Gutmann, D. H., & Guha, A. (1996) · Journal of neurosurgery · doi:10.3171/jns.1996.84.5.0867 · Cited by 36
Expression of proto-oncogenes in neural tissues
Sudol, M. (1988) · Brain Research · doi:10.1016/0006-8993(88)91228-0 · Cited by 36
The carboxy-terminal catalytic domain of the GTPase-activating protein inhibits nuclear signal transduction and morphological transformation mediated by the CSF-1 receptor.Preprint
Bortner, D. M., Ulivi, M., Roussel, M. F., & Ostrowski, M. C. (1991) · Genes & Development · doi:10.1101/gad.5.10.1777 · Cited by 36
The Allosteric Switch and Conformational States in Ras GTPase Affected by Small Molecules
Johnson, C. W., & Mattos, C. (2013) · The Enzymes · doi:10.1016/b978-0-12-416749-0.00003-8 · Cited by 35
SH2 Domain Binding: Diverse FLVRs of Partnership
Chehayeb, R. J., & Boggon, T. J. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.575220 · Cited by 35
Probing the role of loop 2 in Ras function with unnatural amino acids.
Chung, H. H., Benson, D. R., Cornish, V. W., & Schultz, P. G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.10145 · Cited by 35
ras Proto-Oncogene Activation in Human Malignancy
Clark, G. J., & Der, C. J. (1995) · Humana Press eBooks · doi:10.1007/978-1-4757-2381-6_2 · Cited by 35
Dominant Yeast and Mammalian RAS Mutants That Interfere with the CDC25-Dependent Activation of Wild-Type RAS in Saccharomyces cerevisiae
Powers, S., O’Neill, K. E., & Wigler, M. H. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.2.390-395.1989 · Cited by 35
RAS Nanoclusters: Dynamic Signaling Platforms Amenable to Therapeutic Intervention
Van, Q. N., Prakash, P., Shrestha, R., Balius, T. E., Turbyville, T. J., & Stephen, A. G. (2021) · Biomolecules · doi:10.3390/biom11030377 · Cited by 34
Restricted tissue expression pattern of a novel human rasGAP-related gene and its murine ortholog
Allen, M., Chu, S., Brill, S., Stotler, C., & Buckler, A. (1998) · Gene · doi:10.1016/s0378-1119(98)00394-1 · Cited by 34
Detection of K-ras mutations in resected primary leiomyosarcoma.
Hill, M. A., Gong, C., Casey, T. J., Menon, A. G., Mera, R. M., Gillespie, A. T., Giardina, J. F., Levine, E. A., & Hunt, J. D. (1997) · PubMed · Cited by 34
GTPase-dependent signaling in bacteria: characterization of a membrane-binding site for era in Escherichia coli
Lin, Y. P., Sharer, J. D., & March, P. E. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.1.44-49.1994 · Cited by 34
Chromosome localization and cDNA sequence of murine and human genes forras p21 GTPase activating protein (GAP)
Hsieh, C., Vogel, U. S., Dixon, R. A. F., & Francke, U. (1989) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01534919 · Cited by 34
Novel PI3K/Akt/mTOR pathway inhibitors plus radiotherapy: Strategy for non-small cell lung cancer with mutant RAS gene
Chen, K., Shang, Z., Dai, A.-L., & Dai, P.-L. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117816 · Cited by 33
Interaction of GTPase-activating protein with p21ras, measured using a continuous assay for inorganic phosphate release
Webb, M. R., & Hunter, J. L. (1992) · Biochemical Journal · doi:10.1042/bj2870555 · Cited by 33
Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells
Katagiri, K., Hattori, S., Nakamura, S., Yamamoto, T., Yoshida, T., & Katagiri, T. (1994) · Blood · doi:10.1182/blood.v84.6.1780.1780 · Cited by 33
Overexpression of RPI1, a novel inhibitor of the yeast Ras-cyclic AMP pathway, down-regulates normal but not mutationally activated ras function.
Kim, J., & Powers, S. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.8.3894 · Cited by 33

Authors: Trahey, M., & McCormick, F.
Affiliations: Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.
ORCID: McCormick, Frank
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1987-10-23
Volume: 238
Issue: 4826
Pages: 542-545
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2821624
OpenAlex: W2058511768
Cited by: 1,211
References: 23
Citations by year: 2026: 12 · 2025: 19 · 2024: 19 · 2023: 12 · 2022: 12 · 2021: 19 · 2020: 14 · 2019: 9 · 2018: 17 · 2017: 18 · 2016: 20 · 2015: 17 · 2014: 10 · 2013: 9 · 2012: 18
FWCI: 32.07
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
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 › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: GTPase activity, GDP-bound state, GTP hydrolysis, cytosolic proteins, guanine nucleotides
MeSH terms: Animals, Biological Assay, Cytoplasm, Female, Guanine Nucleotides, Guanosine Diphosphate, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Hydrolysis, Immunosorbent Techniques, Mutation, Oocytes, Phosphoric Monoester Hydrolases, Proteins, Proto-Oncogene Proteins, Structure-Activity Relationship, Xenopus laevis, Proto-Oncogene Proteins p21(ras), GTP Phosphohydrolases

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A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants

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