R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways

Marte, Barbara M.; Rodriguez-Viciana, Pablo; Wennström, Stefan; Warne, Patricia H.; Downward, Julian

doi:10.1016/s0960-9822(06)00028-5

Cited by 223Protein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancerCellular transport and secretion

R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways

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Marte, Barbara M., Rodriguez-Viciana, Pablo, Wennström, Stefan, Warne, Patricia H., Downward, Julian·1997·Current Biology

DOI 10.1016/s0960-9822(06)00028-5

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Abstract

Background The small GTPase R-Ras displays a less potent transforming activity than the closely related Ras oncogene products. Although R-Ras has been reported to interact with c-Raf1 and Ral-GDS in vitro, the pathways by which it exerts its effects on cellular proliferation are not known.Results Both Ras and R-Ras interact with phosphoinositide (PI) 3-kinase in vitro, and induce elevation of the levels of PI 3-kinase lipid products in intact cells. Unlike Ras, R-Ras does not activate Raf or mitogen-activated protein (MAP) kinase in cells. In co-transfection assays, the serine/threonine protein kinase PKB (or Akt) is effectively stimulated by R-Ras, Ras, mutants of Ras that activate PI 3-kinase but not other effectors, and activated forms of PI 3-kinase. Ras and R-Ras stimulate PKB/Akt through a non-autocrine mechanism that involves PI 3-kinase. The constitutive activation of PI 3-kinase alone is sufficient to activate PKB/Akt, but not the MAP kinase ERK or the stress-activated protein kinase, Jun N-terminal kinase. Transformation assays in fibroblasts suggest that PKB/Akt and Raf are part of distinct oncogenic signalling pathways.Conclusions Both the Raf-MAP kinase and PI 3-kinase-PKB/Akt pathways are activated by Ras, but only the PI 3-kinase-PKB/Akt pathway is activated by R-Ras. PI 3-kinase, and downstream targets such as PKB/Akt, are likely to be essential mediators of transformation induced by R-Ras. PI 3-kinase, as well as Raf, is thus implicated also in Ras transformation.

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Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244 · see citing works
A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002).
Vlahos, C. J., Matter, W. F., Hui, K. Y., & Brown, R. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37680-9 · Cited by 3,248 · see citing works
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
Burgering, B. M. T., & Coffer, P. J. (1995) · Nature · doi:10.1038/376599a0 · Cited by 2,113 · see citing works
The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
Franke, T. F., Yang, S., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., & Tsichlis, P. N. (1995) · Cell · doi:10.1016/0092-8674(95)90534-0 · Cited by 2,006 · see citing works
Phosphatidylinositol-3-OH kinase direct target of Ras
Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., & Downward, J. (1994) · Nature · doi:10.1038/370527a0 · Cited by 1,954 · see citing works
Self-citation
All ras proteins are polyisoprenylated but only some are palmitoylated
Hancock, J. F., Magee, A. I., Childs, J. E., & Marshall, C. J. (1989) · Cell · doi:10.1016/0092-8674(89)90054-8 · Cited by 1,775 · see citing works
The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
Coso, O. A., Chiariello, M., Yu, J., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Gutkind, J. S. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,629 · see citing works
Selective activation of the JNK signaling cascadeand c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
Minden, A., Lin, A., Claret, F.-X., Abo, A., & Karin, M. (1995) · Cell · doi:10.1016/s0092-8674(05)80019-4 · Cited by 1,481 · see citing works
Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064 · see citing works
Self-citation
Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
Leevers, S. J., Paterson, H. F., & Marshall, C. J. (1994) · Nature · doi:10.1038/369411a0 · Cited by 1,016 · see citing works
Activation of Raf as a Result of Recruitment to the Plasma Membrane
Stokoe, D., Macdonald, S. G., Cadwallader, K. A., Symons, M. H., & Hancock, J. F. (1994) · Science · doi:10.1126/science.7811320 · Cited by 976 · see citing works
Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate.
Nakanishi, H., Brewer, K., & Exton, J. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54107-7 · Cited by 954 · see citing works
A Retroviral Oncogene, akt , Encoding a Serine-Threonine Kinase Containing an SH2-Like Region
Bellacosa, A., Testa, J. R., Staal, S. P., & Tsichlis, P. N. (1991) · Science · doi:10.1126/science.1833819 · Cited by 939 · see citing works
Molecular alterations of the AKT2 oncogene in ovarian and breast carcinomas
Bellacosa, A., de Feo, D., Godwin, A. K., Bell, D. W., Cheng, J. Q., Altomare, D. A., Wan, M., Dubeau, L., Scambia, G., Masciullo, V., et al. (1995) · International Journal of Cancer · doi:10.1002/ijc.2910640412 · Cited by 837 · see citing works
Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA.
Cheng, J. Q., Ruggeri, B., Klein, W. M., Sonoda, G., Altomare, D. A., Watson, D. K., & Testa, J. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3636 · Cited by 793 · see citing works
Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
Warne, P. H., Vician, P. R., & Downward, J. (1993) · Nature · doi:10.1038/364352a0 · Cited by 729 · see citing works
Self-citation
PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase
Chung, J., Grammar, T. C., Lemon, K. P., Kazlauskas, A., & Blenis, J. (1994) · Nature · doi:10.1038/370071a0 · Cited by 719 · see citing works
Activation of phosphoinositide 3‐kinase by interaction with Ras and by point mutation.
Rodriguez‐Viciana, P., Warne, P. H., Vanhaesebroeck, B., Waterfield, M. D., & Downward, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00602.x · Cited by 565 · see citing works
Self-citation
Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3.
Toker, A., Meyer, M., Reddy, K. K., Falck, J. R., Aneja, R., Aneja, S. G., Parra, A., Burns, D. J., Ballas, L. M., & Cantley, L. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31643-0 · Cited by 553 · see citing works
PDGF stimulates an increase in GTP–Rac via activation of phosphoinositide 3-kinase
Hawkins, P. T., Eguinoa, A., Qiu, R., Stokoe, D., Cooke, F. T., Walters, R. J., Wennström, S., Claesson, L., Evans, T., Symons, M. H., et al. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00080-7 · Cited by 536 · see citing works
Self-citation
Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily.
Jones, P. F., Jakubowicz, T., Pitossi, F. J., Maurer, F., & Hemmings, B. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4171 · Cited by 532 · see citing works
Activation of extracellular signal‐regulated kinase, ERK2, by p21ras oncoprotein.
Leevers, S. J., & Marshall, C. J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05088.x · Cited by 496 · see citing works
Molecular cloning and characterisation of a novel putative protein‐serine kinase related to the cAMP‐dependent and protein kinase C families
Coffer, P. J., & Woodgett, J. R. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16305.x · Cited by 493 · see citing works
Akt, a Pleckstrin Homology Domain Containing Kinase, Is Activated Primarily by Phosphorylation
Kohn, A. D., Takeuchi, F., & Roth, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.21920 · Cited by 476 · see citing works
Ras effectors
Marshall, C. J. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80066-4 · Cited by 463 · see citing works
PI 3‐kinase is a dual specificity enzyme: autoregulation by an intrinsic protein‐serine kinase activity.
Dhand, R., Hiles, I., Panayotou, G., Roche, S., Fry, M., Gout, I. T., Totty, N. F., Truong, O., Vicendo, P., & Yonezawa, K. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06290.x · Cited by 446 · see citing works
Membrane Localization of Phosphatidylinositol 3-Kinase Is Sufficient To Activate Multiple Signal-Transducing Kinase Pathways
Klippel, A., Reinhard, C., Kavanaugh, W. M., Apell, G., Escobedo, M.-A., & Williams, L. T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4117 · Cited by 441 · see citing works
Integrin Activation by R-ras
Zhang, Z., Vuori, K., Wang, H., Reed, J. C., & Ruoslahti, E. I. (1996) · Cell · doi:10.1016/s0092-8674(00)81082-x · Cited by 409 · see citing works
Insulin stimulates the kinase activity of RAC‐PK, a pleckstrin homology domain containing ser/thr kinase.
Kohn, A. D., Kovacina, K. S., & Roth, R. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00103.x · Cited by 355 · see citing works
Quantitative Analysis of the Complex between p21 and the Ras-binding Domain of the Human Raf-1 Protein Kinase
Herrmann, C., Martin, G. A., & Wittinghofer, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2901 · Cited by 350 · see citing works
Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
James, S. R., Downes, C. P., Gigg, R., Grove, S. J. A., Holmes, A. B., & Alessi, D. R. (1996) · Biochemical Journal · doi:10.1042/bj3150709 · Cited by 339 · see citing works
Ral‐GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation.
Urano, T., Emkey, R., & Feig, L. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00416.x · Cited by 332 · see citing works
The activation of phosphatidylinositol 3-kinase by Ras
Kodaki, T., Woscholski, R., Hallberg, B., Rodriguez-Viciana Julian Downward, P., & Parker, P. J. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00177-9 · Cited by 329 · see citing works
Characterization of Four Novel ras -Like Genes Expressed in a Human Teratocarcinoma Cell Line
Drivas, G., Shih, A., Coutavas, E. E., Rush, M. G., & D’Eustachio, P. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.4.1793-1798.1990 · Cited by 310 · see citing works
The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1
Galisteo, M. L., Chernoff, J., Su, Y. C., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.35.20997 · Cited by 274 · see citing works
The phosphatidylinositol 3-kinase alpha is required for DNA synthesis induced by some, but not all, growth factors.
Roche, S., Koegl, M., & Courtneidge, S. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9185 · Cited by 267 · see citing works
Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap.
Spaargaren, M., & Bischoff, J. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12609 · Cited by 265 · see citing works
Bcl-2 associates with the ras-related protein R-rasp23
Fernandez-Sarabia, M. J., & Bischoff, J. R. (1993) · Nature · doi:10.1038/366274a0 · Cited by 256 · see citing works
Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins
Garrett, M. D., Self, A. J., van Oers, C., & Hall, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31215-2 · Cited by 252 · see citing works
Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes
Lowe, D. G., Capon, D. J., Delwart, E., Sakaguchi, A. Y., Naylor, S. L., & Goeddel, D. V. (1987) · Cell · doi:10.1016/0092-8674(87)90364-3 · Cited by 208 · see citing works
Rapid induction of heparin-binding epidermal growth factor/diphtheria toxin receptor expression by Raf and Ras oncogenes.Preprint
McCarthy, S. A., Samuels, M. L., Pritchard, C. A., Abraham, J. A., & McMahon, M. (1995) · Genes & Development · doi:10.1101/gad.9.16.1953 · Cited by 194 · see citing works
The drosophila ras oncogenes: Structure and nucleotide sequence
Neuman‐Silberberg, F. S., Schejter, E. D., Hoffmann, F. M., & Shilo, B. (1984) · Cell · doi:10.1016/0092-8674(84)90437-9 · Cited by 180 · see citing works
Direct Interaction between Ras and the Kinase Domain of Mitogen-activated Protein Kinase Kinase Kinase (MEKK1)
Russell, M., Lange, C. A., & Johnson, G. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11757 · Cited by 172 · see citing works
AH/PH Domain-Mediated Interaction between Akt Molecules and Its Potential Role in Akt Regulation
Datta, K., Franke, T. F., Chan, T. O., Makris, A. M., Yang, S.-I., Kaplan, D. R., Morrison, D. K., Golemis, E. A., & Tsichlis, P. N. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.4.2304 · Cited by 164 · see citing works
R-Ras promotes apoptosis caused by growth factor deprivation via a Bcl-2 suppressible mechanism.
Wang, H., Millan, J. A., Cox, A. D., Der, C. J., Rapp, U. R., Beck, T., Zha, H., & Reed, J. C. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.4.1103 · Cited by 149 · see citing works
Platelet-Derived Growth Factor-Dependent Activation of Phosphatidylinositol 3-Kinase Is Regulated by Receptor Binding of SH2-Domain-Containing Proteins Which Influence Ras Activity
Klinghoffer, R. A., Duckworth, B. C., Valius, M., Cantley, L. C., & Kazlauskas, A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5905 · Cited by 134 · see citing works
R-Ras induces malignant, but not morphologic, transformation of NIH3T3 cells.
Cox, A. D., Brtva, T. R., Lowe, D. G., & Der, C. J. (1994) · PubMed · Cited by 111 · see citing works
A role for phosphatidylinositol 3-kinase in the regulation of beta 1 integrin activity by the CD2 antigen.
Shimizu, Y., Mobley, J. L., Finkelstein, L. D., et al. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.6.1867 · Cited by 110 · see citing works
Oncogenic activation of human R-ras by point mutations analogous to those of prototype H-ras oncogenes.
Sáez, R., Chan, A. M.-L., Miki, T., & Aaronson, S. A. (1994) · PubMed · Cited by 81 · see citing works
Ionizing Radiation Stimulates a Grb2-mediated Association of the Stress-activated Protein Kinase with Phosphatidylinositol 3-Kinase
Kharbanda, S. M., Saleem, A., Shafman, T. D., Emoto, Y., Taneja, N., Rubin, E. H., Weichselbaum, R. R., Woodgett, J. R., Avruch, J., Kyriakis, J. M., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18871 · Cited by 74 · see citing works
Heterologous expression and characterization of the human R-ras gene product.
Lowe, D. G., & Goeddel, D. V. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2845 · Cited by 73 · see citing works
Complexes of p21RAS with JUN N-terminal kinase and JUN proteins.
Adler, V., Pincus, M. R., Brandt‐Rauf, P. W., & Ronai, Z. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10585 · Cited by 71 · see citing works
R-ras interacts with rasGAP, neurofibromin and c-raf but does not regulate cell growth or differentiation.
Rey, I., Taylor-Harris, P. M., van Erp, H., & Hall, A. (1994) · PubMed · Cited by 64 · see citing works
The Ras-related protein R-ras interacts directly with Raf-1 in a GTP-dependent manner
Spaargaren, M., Martin, G. A., McCormick, F. P., Fernandez-Sarabia, M. J., & Bischoff, J. R. (1994) · Biochemical Journal · doi:10.1042/bj3000303 · Cited by 63 · see citing works
Quail neuroretina c-Rmil(B-raf) proto-oncogene cDNAs encode two proteins of 93.5 and 95 kDa resulting from alternative splicing.
Eychène, A., Barnier, J., Dezélée, P., et al. (1992) · PubMed · Cited by 25 · see citing works

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Authors: Marte, B. M., Rodriguez-Viciana, P., Wennström, S., Warne, P. H., & Downward, J.
Corresponding author: Downward, Julian
ORCID: Wennström, Stefan
Downward, Julian
Venue: Current Biology
Publisher: Elsevier BV
Published: 1997-01
Volume: 7
Issue: 1
Pages: 63-71
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/s0960-9822(06)00028-5
OpenAlex: W2074830772
Cited by: 223
References: 55
Citations by year: 2026: 3 · 2024: 6 · 2023: 2 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 2 · 2014: 7 · 2013: 4 · 2012: 4
FWCI: 9.60
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6041 d)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: National Institutes of Health
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 › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: R-Ras, oncogenic Ras, phosphatidylinositol 3-kinase, Akt, Ras transformation, oncogenic signalling pathways, ERK, JNK, fibroblast transformation
MeSH terms: Animals, Cell Transformation, Neoplastic, Enzyme Activation, Gene Expression Regulation, Neoplastic, Phosphotransferases (Alcohol Group Acceptor), Calcium-Calmodulin-Dependent Protein Kinases, ras Proteins, Phosphatidylinositol 3-Kinases, GTP Phosphohydrolases, Mice

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R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways

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