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

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Gibbs, J. B., Proceedings of the National Academy of Sciences of the United States of America 81: 5704 (1984).
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Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases
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Thomas, S. Μ., DeMarco, M., D’Arcangelo, G., Halegoua, S., & Brugge, J. S. (1992) · Cell · doi:10.1016/0092-8674(92)90075-n · Cited by 676
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Vogel, U. S., Dixon, R. A. F., Schaber, M. D., Diehl, R. E., Marshall, M. S., Scolnick, E. M., Sigal, I. S., & Gibbs, W. W. (1988) · Nature · doi:10.1038/335090a0 · Cited by 649
Multistage carcinogenesis in mouse skin
DiGiovanni, J. (1992) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(92)90051-z · Cited by 646
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Serafini, T. A., Orci, L., AMHERDT, M., Brunner, M., Kahn, R., & Rothmant, J. E. (1991) · Cell · doi:10.1016/0092-8674(91)90176-y · Cited by 609
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Zhu, Y., Romero‐Ortega, M. I., Ghosh, P., Ye, Z., Charnay, P., Rushing, E. J., Marth, J. D., & Parada, L. F. (2001) · Genes & Development · doi:10.1101/gad.862101 · Cited by 606
Abnormal regulation of mammalian p21ras contributes to malignant tumor growth in von Recklinghausen (type 1) neurofibromatosis
DeClue, J. E., Papageorge, A. G., Fletcher, J. A., Diehl, S. R., Ratner, N., Vass, W. C., & Lowy, D. R. (1992) · Cell · doi:10.1016/0092-8674(92)90407-4 · Cited by 580
The ras protein family: evolutionary tree and role of conserved amino acids
Valencia, A., Chardin, P., Wittinghofer, A., & Sander, C. (1991) · Biochemistry · doi:10.1021/bi00233a001 · Cited by 569
The superoxide‐generating oxidase of phagocytic cells
Morel, F., Doussière, J., & Vignais, P. V. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16312.x · Cited by 565
The pathway to signal achievement
Egan, S. E., & Weinberg, R. A. (1993) · Nature · doi:10.1038/365781a0 · Cited by 560
Ras-Dependent Induction of Cellular Responses by Constitutively Active Phosphatidylinositol-3 Kinase
Hu, Q., Klippel, A., Muslin, A. J., Fantl, W. J., & Williams, L. T. (1995) · Science · doi:10.1126/science.7701328 · Cited by 547
Pan-KRAS Inhibitor Disables Oncogenic Signalling and Tumour Growth
Kim, D., Herdeis, L., Rudolph, D., Zhao, Y., Böttcher, J., Vides, A., Ayala-Santos, C. I., Pourfarjam, Y., Cuevas-Navarro, A., Xue, J. Y., et al. (2023) · Nature · doi:10.1038/s41586-023-06123-3 · Cited by 534
Asparagine residue in the rho Gene Product Is the Modification Site for Botulinum ADP-ribosyltransferase
Sekine, A., Fujiwara, M., & Narumiya, S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81834-8 · Cited by 541
Ras Protein Farnesyltransferase: A Strategic Target for Anticancer Therapeutic Development
Rowinsky, E. K., Windle, J. J., & Hoff, D. D. V. (1999) · Journal of Clinical Oncology · doi:10.1200/jco.1999.17.11.3631 · Cited by 533
SIGNALING PATHWAYS IN INTESTINAL DEVELOPMENT AND CANCER
Sancho, E., Batlle, E., & Clevers, H. C. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.092805 · Cited by 560
Genetic and Pharmacological Suppression of Oncogenic Mutations in RAS Genes of Yeast and Humans
Schafer, W. R., Kim, R., Sterne, R. E., Thorner, J. W., Kim, S., & Rine, J. (1989) · Science · doi:10.1126/science.2569235 · Cited by 530
PDGF β-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex
Kaplan, D. R., Morrison, D. K., Wong, G. A., McCormick, F. P., & Williams, L. T. (1990) · Cell · doi:10.1016/0092-8674(90)90220-9 · Cited by 519
Self-citation
Small GTP-Binding Proteins
Takai, Y., Kaibuchi, K., Kikuchi, A., & Kawata, M. (1992) · International review of cytology · doi:10.1016/s0074-7696(08)61861-6 · Cited by 509
Guanosine Triphosphatase Activating Protein (GAP) Interacts with the p21 ras Effector Binding Domain
Adari, H. Y., Lowy, D. R., Willumsen, B. M., Der, C. J., & McCormick, F. P. (1988) · Science · doi:10.1126/science.2833817 · Cited by 506
Self-citation
Vascular Endothelial Cell Growth Factor Promotes Tyrosine Phosphorylation of Mediators of Signal Transduction That Contain SH2 Domains
Guo, D., Jia, Q., Song, H.-Y., Warren, R. S., & Donner, D. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.12.6729 · Cited by 482
Bcr encodes a GTPase-activating protein for p21rac
Diekmann, D., Brill, S., Garrett, M. D., Totty, N. F., Hsuan, J. J., Monfries, C. A. L., Hall, C., Lim, L., & Hall, A. (1991) · Nature · doi:10.1038/351400a0 · Cited by 477
Molecular Cloning of Two Types of GAP Complementary DNA from Human Placenta
Trahey, M., Wong, G. A., Halenbeck, R., Rubinfeld, B., Martin, G. A., Ladner, M. B., Long, C. M., Crosier, W. J., Watt, K., Koths, K. E., et al. (1988) · Science · doi:10.1126/science.3201259 · Cited by 442
Self-citation
Src homology region 2 domains direct protein-protein interactions in signal transduction.
Moran, M. F., Koch, C. A., Anderson, D. M., Ellis, C. A., England, L. J., Martin, G. S., & Pawson, T. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8622 · Cited by 462
PDGF induction of tyrosine phosphorylation of GTPase activating protein
Molloy, C. J., Bottaro, D. P., Fleming, T. P., Marshall, M. S., Gibbs, W. W., & Aaronson, S. A. (1989) · Nature · doi:10.1038/342711a0 · Cited by 454
Phospholipase C-β1 is a GTPase-activating protein for Gq/11, its physiologic regulator
Berstein, G., Blank, J. L., Jhon, D.-Y., Exton, J. H., Rhee, S. G., & Ross, E. M. (1992) · Cell · doi:10.1016/0092-8674(92)90165-9 · Cited by 428
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter, S. M., Valenzuela, D., Kennedy, T. E., Neer, E. J., & Fishman, M. C. (1990) · Nature · doi:10.1038/344836a0 · Cited by 420
The let-23 gene necessary for Caenorhabditis elegans vulval induction encodes a tyrosine kinase of the EGF receptor subfamily
Aroian, R. V., Koga, M., Mendel, J., Ohshima, Y., & Sternberg, P. W. (1990) · Nature · doi:10.1038/348693a0 · Cited by 416
GTPase-activating proteins: Helping hands to complement an active site
Scheffzek, K., Ahmadian, M. R., & Wittinghofer, A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01224-9 · Cited by 410
Function of Ras as a molecular switch in signal transduction.
Satoh, T., Nakafuku, M., & Kaziro, Y. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35739-9 · Cited by 409
Digital signaling and hysteresis characterize Ras activation in lymphoid cells.
Das, J., Ho, M., Zikherman, J., Govern, C., Yang, M., Weiss, A., Chakraborty, A. K., & Roose, J. P. (2009) · Cell · doi:10.1016/j.cell.2008.11.051 · Cited by 398
Somatic mutations in the neurofibromatosis 1 gene in human tumors
Li, Y., Bollag, G. E., Clark, R., Stevens, J., Conroy, L., Fults, D., Ward, K., Friedman, E., Samowitz, W. S., Robertson, M. A., et al. (1992) · Cell · doi:10.1016/0092-8674(92)90408-5 · Cited by 394
Self-citation
let-60, a gene that specifies cell fates during C. elegans vulval induction, encodes a ras protein
Han, M., & Sternberg, P. W. (1990) · Cell · doi:10.1016/0092-8674(90)90495-z · Cited by 394
Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules
Krengel, U., Schlichting, I., Scherer, A., Schumann, R., Frech, M., John, J., Kabsch, W., PAI, E. F., & Wittinghofer, A. (1990) · Cell · doi:10.1016/0092-8674(90)90018-a · Cited by 386
cDNA cloning of the type 1 neurofibromatosis gene: Complete sequence of the NF1 gene product
Marchuk, D. A., Saulino, A. M., Tavakkol, R., Swaroop, M., Wallace, M. R., Andersen, L. B., Mitchell, A. L., Gutmann, D. H., Boguski, M. S., & Collins, F. S. (1991) · Genomics · doi:10.1016/0888-7543(91)90017-9 · Cited by 390
The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product
Calés, C., Hancock, J. F., Marshall, C. J., & Hall, A. (1988) · Nature · doi:10.1038/332548a0 · Cited by 386
Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
Ahmadian, M. R., Stege, P., Scheffzek, K., & Wittinghofer, A. (1997) · Nature Structural Biology · doi:10.1038/nsb0997-686 · Cited by 370
ADP-ribosylation factor is functionally and physically associated with the Golgi complex.
Stearns, T., Willingham, M. C., Botstein, D., & Kahn, R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.3.1238 · Cited by 372
Binding of GAP to Activated PDGF Receptors
Kazlauskas, A., Ellis, C. A., Pawson, T. J., & Cooper, J. A. (1990) · Science · doi:10.1126/science.2157284 · Cited by 369
The RHO Family GTPases: Mechanisms of Regulation and Signaling
Mosaddeghzadeh, N., & Ahmadian, M. R. (2021) · Cells · doi:10.3390/cells10071831 · Cited by 385
p62 : A Constitutively Tyrosine-Phosphorylated, GAP-Associated Protein in Chronic Myelogenous Leukemia Progenitor Cells
Carpino, N., Wisniewski, D. J., Strife, A., Marshak, D. R., Kobayashi, R., Stillman, B., & Clarkson, B. D. (1997) · Cell · doi:10.1016/s0092-8674(00)81840-1 · Cited by 366
Post‐translational processing of p21ras is two‐step and involves carboxyl‐methylation and carboxy‐terminal proteolysis.
Gutierrez, L., Magee, A. I., Marshall, C. J., & Hancock, J. F. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03478.x · Cited by 460
Ras Conformational Ensembles, Allostery, and Signaling
Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355
RapV12 antagonizes Ras‐dependent activation of ERK1 and ERK2 by LPA and EGF in Rat‐1 fibroblasts.
Cook, S. J., Rubinfeld, B., Albert, I., & McCormick, F. P. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06022.x · Cited by 348
Self-citation
Cell cycle tyrosine phosphorylation of p34cdc2 and a microtubule-associated protein kinase homolog in Xenopus oocytes and eggs.
Ferrell, J. E., Wu, M. W., Gerhart, J. C., & Martin, G. S. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.1965 · Cited by 346
Differential regulation of rasGAP and neurofibromatosis gene product activities
Bollag, G. E., & McCormick, F. P. (1991) · Nature · doi:10.1038/351576a0 · Cited by 341
Self-citation
Farnesol modification of Kirsten-ras exon 4B protein is essential for transformation.
Jackson, J. H., Cochrane, C. G., Bourne, J. R., Solski, P. A., Buss, J. E., & Der, C. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.3042 · Cited by 338
Molecular cloning of cDNAs encoding the GAP-associated protein p190: Implications for a signaling pathway from ras to the nucleus
Settleman, J. E., Narasimhan, V., Foster, L. C., & Weinberg, R. A. (1992) · Cell · doi:10.1016/0092-8674(92)90454-k · Cited by 333
Purification of a RAS -Responsive Adenylyl Cyclase Complex from Saccharomyces cerevisiae by Use of an Epitope Addition Method
Field, J. M., Nikawa, J., Broek, D., MACDONALD, B. S., Rodgers, L., Wilson, I. A., Lerner, R. A., & Wigler, M. H. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.5.2159-2165.1988 · Cited by 330
Multiple K-ras codon 12 mutations in cholangiocarcinomas demonstrated with a sensitive polymerase chain reaction technique.
Levi, S., Urbano-Ispizúa, Á., Gill, R., Thomas, D. M., Gilbertson, J. A., Foster, C., & Marshall, C. J. (1991) · PubMed · Cited by 328
Interaction of the Nuclear GTP-Binding Protein Ran with Its Regulatory Proteins RCC1 and RanGAP1
Klebe, C., Bischoff, F. R., Ponstingl, H., & Wittinghofer, A. (1995) · Biochemistry · doi:10.1021/bi00002a031 · Cited by 323
Structure-based assignment of the biochemical function of a hypothetical protein: A test case of structural genomics
Zarembinski, T. I., Hung, L., Müller-Dieckmann, H.-J., Kim, K.-K., Yokota, H. A., Kim, R., & Kim, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15189 · Cited by 323
Therapeutic Strategies for Targeting Ras Proteins
Gysin, S., Salt, M. B., Young, A. E., & McCormick, F. (2011) · Genes & Cancer · doi:10.1177/1947601911412376 · Cited by 329
Self-citation
S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase activating protein
Tanaka, K., Nakafuku, M., Satoh, T., Marshall, M. S., Gibbs, W. W., Matsumoto, K., Kaziro, Y., & Toh‐e, A. (1990) · Cell · doi:10.1016/0092-8674(90)90094-u · Cited by 323
Mutational analysis of SEC4 suggests a cyclical mechanism for the regulation of vesicular traffic.
Walworth, N. C., Goud, B., Kabcenell, A. K., & Novick, P. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03560.x · Cited by 312
The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain
Reneke, J. E., Blumer, K., Courchesne, W. E., & Thorner, J. W. (1988) · Cell · doi:10.1016/0092-8674(88)90045-1 · Cited by 311

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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