Cited by 327Protein Kinase Regulation and GTPase SignalingCellular transport and secretionProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 82 of the 82 references it cites were found in a registry or an index.

Signaling Specificity by Ras Family GTPases Is Determined by the Full Spectrum of Effectors They Regulate

Open access

Rodriguez-Viciana, Pablo, Sabatier, Celine, McCormick, Frank·2004·Molecular and Cellular Biology

DOI 10.1128/mcb.24.11.4943-4954.2004PMC PMC416418

Open this paper in CoChat — free account

Abstract

Ras family GTPases (RFGs) regulate signaling pathways that control multiple biological processes. How signaling specificity among the closely related family members is achieved is poorly understood. We have taken a proteomics approach to signaling by RFGs, and we have analyzed interactions of a panel of RFGs with a comprehensive group of known and potential effectors. We have found remarkable differences in the ability of RFGs to regulate the various isoforms of known effector families. We have also identified several proteins as novel effectors of RFGs with differential binding specificities to the various RFGs. We propose that specificity among RFGs is achieved by the differential regulation of combinations of effector families as well as by the selective regulation of different isoforms within an effector family. An understanding of this new level of complexity in the signaling pathways regulated by RFGs is necessary to understand how they carry out their many cellular functions. It will also likely have critical implications in the treatment of human diseases such as cancer.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1128/mcb.24.11.4943-4954.2004

Cites

82 of 82 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

ras oncogenes in human cancer: a review.
Bos, J. L. (1989) · PubMed · Cited by 5,061
Small GTP-Binding Proteins
Takai, Y., Sasaki, T., & Matozaki, T. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.1.153 · Cited by 2,511
Cellular Function of Phosphoinositide 3-Kinases: Implications for Development, Immunity, Homeostasis, and Cancer
Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J. F., & Waterfield, M. D. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.615 · Cited by 1,234
FUNCTION AND REGULATION OF RAS
Lowy, D. R., & Willumsen, B. M. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004223 · Cited by 1,164
Epigenetic inactivation of a RAS association domain family protein from the lung tumour suppressor locus 3p21.3
Dammann, R., Li, C., Yoon, J., Chin, P. L., Bates, S., & Pfeifer, G. P. (2000) · Nature Genetics · doi:10.1038/77083 · Cited by 1,064
Raf-Induced Proliferation or Cell Cycle Arrest Is Determined by the Level of Raf Activity with Arrest Mediated by p21Cip1
Woods, D. B., Parry, D., Cherwinski, H. M., Bosch, E., Lees, E. M., & McMahon, M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5598 · Cited by 639
Rap1 signalling: adhering to new models
Bos, J. L., de Rooij, J., & Reedquist, K. A. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35073073 · Cited by 625
A novel Epac-specific cAMP analogue demonstrates independent regulation of Rap1 and ERK
Enserink, J. M., Christensen, A. E., de Rooij, J., van Triest, M., Schwede, F., Genieser, H. G., Døskeland, S. O., Blank, J. L., & Bos, J. L. (2002) · Nature Cell Biology · doi:10.1038/ncb874 · Cited by 625
Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ
Pacold, M. E., Suire, S., Perišić, O., Lara‐González, S., Davis, C. T., Walker, E. H., Hawkins, P. T., Stephens, L., Eccleston, J. F., & Williams, R. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00196-3 · Cited by 611
Phosphatidylinositol-3-OH kinases are Rab5 effectors
Christoforidis, S., Miaczynska, M., Ashman, K., Wilm, M., Zhao, L., Yip, S.-C., Waterfield, M. D., Backer, J. M., & Zerial, M. (1999) · Nature Cell Biology · doi:10.1038/12075 · Cited by 559
High-Intensity Raf Signal Causes Cell Cycle Arrest Mediated by p21 Cip1
Sewing, A., Wiseman, B. S., Lloyd, A. C., & Land, H. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5588 · Cited by 457
Differential Regulation of Raf-1, A-Raf, and B-Raf by Oncogenic Ras and Tyrosine Kinases
Marais, R., Light, Y., Paterson, H. F., Mason, C., & Marshall, C. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4378 · Cited by 455
Distinct requirements for Ras oncogenesis in human versus mouse cellsPreprint
Hamad, N. M., Elconin, J. H., Karnoub, A. E., Bai, W., Rich, J. N., Abraham, R. T., Der, C. J., & Counter, C. M. (2002) · Genes & Development · doi:10.17615/zkd7-3774 · Cited by 439
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
Mechanisms of regulating the Raf kinase family
Kopera, H. C., Vikis, H. G., & Guan, K. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00139-0 · Cited by 404
Phospholipase Cϵ: a novel Ras effector
Kelley, G. G., Reks, S. E., Ondrako, J. M., & Smrcka, A. V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.743 · Cited by 361
Identification of a Novel Ras-Regulated Proapoptotic Pathway
Khokhlatchev, A. V., Rabizadeh, S., Xavier, R. J., Nedwidek, M., Chen, T., Zhang, X., Seed, B., & Avruch, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00683-8 · Cited by 358
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
Tiam1 mediates Ras activation of Rac by a PI(3)K-independent mechanism
Lambert, J. M., Lambert, Q. T., Reuther, G. W., Malliri, A., Siderovski, D. P., Sondek, J., Collard, J. G., & Der, C. J. (2002) · Nature Cell Biology · doi:10.1038/ncb833 · Cited by 326
Ras‐activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1
Tall, G. G., Barbieri, M. A., Stahl, P. D., & Horazdovsky, B. F. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00008-9 · Cited by 308
A growing family of guanine nucleotide exchange factors is responsible for activation of ras-family GTPases
Quilliam, L. A., Rebhun, J. F., & Castro, A. F. (2002) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(02)71047-7 · Cited by 286
Heterodimeric Phosphoinositide 3-Kinase Consisting of p85 and p110β Is Synergistically Activated by the βγ Subunits of G Proteins and Phosphotyrosyl Peptide
Kurosu, H., Maehama, T., Okada, T., Yamamoto, T., Hoshino, S.-I., Fukui, Y., Ui, M., Hazeki, O., & Katada, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24252 · Cited by 260
Ral-GTPases: approaching their 15 minutes of fame.
Feig, L. A. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(03)00152-1 · Cited by 249
Conditionally Oncogenic Forms of the A-Raf and B-Raf Protein Kinases Display Different Biological and Biochemical Properties in NIH 3T3 Cells
Pritchard, C. A., Samuels, M. L., Bosch, E., & McMahon, M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.11.6430 · Cited by 224
Roles of Non-catalytic Subunits in Gβγ-induced Activation of Class I Phosphoinositide 3-Kinase Isoforms β and γ
Maier, U., Babich, A., & Nürnberg, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.29311 · Cited by 223
R-Ras can activate the phosphoinositide 3-kinase but not the MAP kinase arm of the Ras effector pathways
Marte, B. M., Rodriguez-Viciana, P., Wennström, S., Warne, P. H., & Downward, J. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00028-5 · Cited by 223
Self-citation
Extracellular signal‐regulated activation of Rap1 fails to interfere in Ras effector signalling
Zwartkruis, F. J. T., Wolthuis, R. M. F., Nabben, N. M. J. M., Franke, B., & Bos, J. L. (1998) · The EMBO Journal · doi:10.1093/emboj/17.20.5905 · Cited by 218
The role of Rap1 in integrin-mediated cell adhesion
Bos, J. L., de Bruyn, K., Enserink, J. M., Kuiperij, H. B., Rangarajan, S., Rehmann, H., Riedl, J., de Rooij, J., van Mansfeld, F., & Zwartkruis, F. J. T. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310083 · Cited by 214
The putative tumor suppressor RASSF1A homodimerizes and heterodimerizes with the Ras-GTP binding protein Nore1
Ortiz-Vega, S., Khokhlatchev, A. V., Nedwidek, M., Zhang, X., Dammann, R., Pfeifer, G. P., & Avruch, J. (2002) · Oncogene · doi:10.1038/sj.onc.1205192 · Cited by 209
A novel family ofras-binding domains
Ponting, C. P., & Benjamin, D. R. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30038-8 · Cited by 205
Does Rap1 deserve a bad Rap?
Stork, P. A. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00087-2 · Cited by 195
Ras and relatives—job sharing and networking keep an old family together
Ehrhardt, A., Ehrhardt, G. R. A., Guo, X., & Schrader, J. W. (2002) · Experimental Hematology · doi:10.1016/s0301-472x(02)00904-9 · Cited by 184
The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functions
Han, D. C., Shen, T., & Guan, J. (2001) · Oncogene · doi:10.1038/sj.onc.1204775 · Cited by 175
Rin, a Neuron-Specific and Calmodulin-Binding Small G-Protein, and Rit Define a Novel Subfamily of Ras Proteins
Lee, C.-H. J., Della, N. G., Chew, C. E., & Zack, D. J. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-21-06784.1996 · Cited by 164
[29] Assay and expression of mitogen-activated protein kinase, MAP kinase kinase, and Raf
Alessi, D. R., Cohen, P., Ashworth, A., Cowley, S. A., Leevers, S. J., & Marshall, C. J. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(95)55031-3 · Cited by 158
Cysteine-rich Region of Raf-1 Interacts with Activator Domain of Post-translationally Modified Ha-Ras
Hu, C., Kariya, K., Tamada, M., Akasaka, K., Shirouzu, M., Yokoyama, S., & Kataoka, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30274 · Cited by 153
The Effect of Posttranslational Modifications on the Interaction of Ras2 with Adenylyl Cyclase
Kuroda, Y., Suzuki, N., & Kataoka, T. (1993) · Science · doi:10.1126/science.8430318 · Cited by 143
Thermodynamic and Kinetic Characterization of the Interaction between the Ras Binding Domain of AF6 and Members of the Ras Subfamily
Linnemann, T., Geyer, M., Jaitner, B. K., Block, C., Kalbitzer, H. R., Wittinghofer, A., & Herrmann, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13556 · Cited by 135
NORE1A, a homologue of RASSF1A tumour suppressor gene is inactivated in human cancers
Hesson, L. B., Dallol, A., Minna, J. D., Maher, E. R., & Latif, F. (2003) · Oncogene · doi:10.1038/sj.onc.1206191 · Cited by 130
14-3-3 Antagonizes Ras-Mediated Raf-1 Recruitment to the Plasma Membrane To Maintain Signaling Fidelity
Light, Y., Paterson, H., & Marais, R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.14.4984-4996.2002 · Cited by 129
An Intact Raf Zinc Finger Is Required for Optimal Binding to Processed Ras and for Ras-Dependent Raf Activation In Situ
Luo, Z., Diaz, B., Marshall, M. S., & Avruch, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.46 · Cited by 123
M-Ras/R-Ras3, a Transforming Ras Protein Regulated by Sos1, GRF1, and p120 Ras GTPase-activating Protein, Interacts with the Putative Ras Effector AF6
Quilliam, L. A., Castro, A. F., Rogers-Graham, K. S., Martin, C. B., Der, C. J., & Bi, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23850 · Cited by 119
Selective Activation of MEK1 but Not MEK2 by A-Raf from Epidermal Growth Factor-stimulated Hela Cells
Wu, X., Noh, S. J., Zhou, G., Dixon, J. E., & Guan, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.3265 · Cited by 119
Protein binding and signaling properties of RIN1 suggest a unique effector function
Han, L., Wong, D., Dhaka, A., Afar, D., White, M. A., Xie, W., Herschman, H. R., Witte, O. N., & Colicelli, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.4954 · Cited by 114
Mechanism of the spatio‐temporal regulation of Ras and Rap1
Ohba, Y., Kurokawa, K., & Matsuda, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg087 · Cited by 112
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
Elucidation of Binding Determinants and Functional Consequences of Ras/Raf-Cysteine-rich Domain Interactions
Williams, J. G., Drugan, J. K., Yi, G. S., Clark, G. J., Der, C. J., & Campbell, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000397200 · Cited by 109
Identification and Characterization of RA-GEF-2, a Rap Guanine Nucleotide Exchange Factor That Serves as a Downstream Target of M-Ras
Gao, X., Satoh, T., Liao, Y., Song, C., Hu, C.-D., Kariya, K.-I., & Kataoka, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105760200 · Cited by 106
Analysis of R-Ras signalling pathways
Self, A. J., Caron, E., Paterson, H. F., & Hall, A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.7.1357 · Cited by 101
The Bcr Kinase Downregulates Ras Signaling by Phosphorylating AF-6 and Binding to Its PDZ Domain
Radziwill, G., Erdmann, R. A., Margelisch, U., & Moelling, K. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.13.4663-4672.2003 · Cited by 98
Aberrant Function of the Ras-Related Protein TC21/R-Ras2 Triggers Malignant Transformation
Graham, S. M., Cox, A. D., Drivas, G., Rush, M. G., D’Eustachio, P., & Der, C. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.4108-4115.1994 · Cited by 97
A human oncogene of the RAS superfamily unmasked by expression cDNA cloning.
Chan, A. M.-L., Miki, T., Meyers, K. A., & Aaronson, S. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7558 · Cited by 94
Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution
Kimmelman, A. C., Tolkacheva, T., Lorenzi, M. V., Osada, M., & Chan, A. M.-L. (1997) · Oncogene · doi:10.1038/sj.onc.1201674 · Cited by 91
Overexpression of the Ras-related TC21/R-Ras2 protein may contribute to the development of human breast cancers.
Clark, G. J., Kinch, M. S., Gilmer, T. M., Burridge, K., & Der, C. J. (1996) · PubMed · Cited by 88
Measurement of GTP-bound Ras-like GTPases by activation-specific probes
van Triest, M., de Rooij, J., & Bos, J. L. (2001) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(01)33068-9 · Cited by 84
Activation of the Raf/MAP kinase cascade by the Ras‐related protein TC21 is required for the TC21‐mediated transformation of NIH 3T3 cells
Rosário, M., Paterson, H. F., & Marshall, C. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1270 · Cited by 83
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
A Novel RalGEF-like Protein, RGL3, as a Candidate Effector for Rit and Ras
Shao, H., & Andres, D. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61461-4 · Cited by 78
Biochemical Characterization of the Ras-Related GTPases Rit and Rin
Shao, H., Kadono‐Okuda, K., Finlin, B. S., & Andres, D. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1448 · Cited by 75
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
A novel RalGEF-like protein, RGL3, as a candidate effector for rit and Ras.
Shao, H., & Andres, D. (2000) · PubMed · doi:10.1074/jbc.m002241200 · Cited by 72
TC21 and Ras share indistinguishable transforming and differentiating activities
Graham, S. M., Oldham, S., Martin, C. B., Drugan, J. K., Zohn, I. E., Campbell, S. L., & Der, C. J. (1999) · Oncogene · doi:10.1038/sj.onc.1202517 · Cited by 72
Association of Yeast Adenylyl Cyclase with Cyclase-Associated Protein CAP Forms a Second Ras-Binding Site Which Mediates Its Ras-Dependent Activation
Shima, F., Okada, T., Kido, M., Sen, H., Tanaka, Y. R., Tamada, M., Hu, C., Yamawaki‐Kataoka, Y., Kariya, K., & Kataoka, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.1.26-33.2000 · Cited by 68
Activation of the Ral and Phosphatidylinositol 3′ Kinase Signaling Pathways by the Ras-Related Protein TC21
Rosário, M., Paterson, H. F., & Marshall, C. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.11.3750-3762.2001 · Cited by 67
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
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
Self-citation
TC21 mediates transformation and cell survival via activation of phosphatidylinositol 3-kinase/Akt and NF-κB signaling pathway
Rong, R., He, Q., Liu, Y., Sheikh, M. S., & Huang, Y. K. (2002) · Oncogene · doi:10.1038/sj.onc.1205154 · Cited by 60
Ras-related TC21 is activated by mutation in a breast cancer cell line, but infrequently in breast carcinomas in vivo
Barker, K. T., & Crompton, M. (1998) · British Journal of Cancer · doi:10.1038/bjc.1998.490 · Cited by 58
Involvement of Phosphatidylinositol 3-Kinase, but Not RalGDS, in TC21/R-Ras2-mediated Transformation
Murphy, G. A., Graham, S. M., Morita, S., Reks, S. E., Rogers-Graham, K., Vojtek, A. B., Kelley, G. G., & Der, C. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109059200 · Cited by 57
Induction of Neurite Extension and Survival in Pheochromocytoma Cells by the Rit GTPase
Spencer, M. L., Shao, H., & Andres, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201092200 · Cited by 56
M-Ras, a Widely Expressed 29-kD Homologue of p21 Ras: Expression of a Constitutively Active Mutant Results in Factor-Independent Growth of an Interleukin-3–Dependent Cell Line
Ehrhardt, G. R. A., Leslie, K. B., Lee, F., Wieler, J. S., & Schrader, J. W. (1999) · Blood · doi:10.1182/blood.v94.7.2433.419k31_2433_2444 · Cited by 54
R-Ras3/M-Ras Induces Neuronal Differentiation of PC12 Cells through Cell-Type-Specific Activation of the Mitogen-Activated Protein Kinase Cascade
Kimmelman, A. C., Rodriguez, N. J. N., & Chan, A. M.-L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5946-5961.2002 · Cited by 54
Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins
Movilla, N., Crespo, P., & Bustelo, X. R. (1999) · Oncogene · doi:10.1038/sj.onc.1202968 · Cited by 54
Guanine nucleotide binding properties of the mammalian RalA protein produced in Escherichia coli.
Frech, M., Schlichting, I., Wittinghofer, A., & Chardin, P. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39333-0 · Cited by 53
Rit, a non-lipid-modified Ras-related protein, transforms NIH3T3 cells without activating the ERK, JNK, p38 MAPK or PI3K/Akt pathways
Rusyn, E. V., Reynolds, E. R., Shao, H., Grana, T. M., Chan, T. O., Andres, D., & Cox, A. D. (2000) · Oncogene · doi:10.1038/sj.onc.1203836 · Cited by 50
A novel insertional mutation in the TC21 gene activates its transforming activity in a human leiomyosarcoma cell line.
Huang, Y., Saez, R., Chao, L., Santos, E., Aaronson, S. A., & Chan, A. M.-L. (1995) · PubMed · Cited by 49
A novel potential effector of M-Ras and p21 Ras negatively regulates p21 Ras-mediated gene induction and cell growth
Ehrhardt, G. R. A., Korherr, C., Wieler, J. S., Knaus, M., & Schrader, J. W. (2001) · Oncogene · doi:10.1038/sj.onc.1204053 · Cited by 41
Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras
高, 賢. (2002) · Kobe University Repository Kernel (Kobe University) · Cited by 34
Identification and Characterization of Mutations in Ha-Ras That Selectively Decrease Binding to cRaf-1
Winkler, D. G., Johnson, J. C., Cooper, J. A., & Vojtek, A. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24402 · Cited by 29
Positive regulation of skeletal myogenesis by R-Ras
Suzuki, J., Kaziro, Y., & Koide, H. (2000) · Oncogene · doi:10.1038/sj.onc.1203402 · Cited by 24
Ras and rap 1 interaction with af-6 effector target
Boettner, B., Herrmann, C., & Aelst, L. V. (2001) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(01)32199-7 · Cited by 18
Ras activation of phosphatidylinositol 3-kinase and akt
Rodriguez‐Viciana, P., & Downward, J. (2001) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(01)33042-2 · Cited by 17
Self-citation

Research works printed but not linked: 2

10.1101/gad.993902 · DOI
10.1128/mcb.7.8.2845-2856.1987 · DOI

Sorted by citations

Ras, PI(3)K and mTOR signalling controls tumour cell growth
Shaw, R. J., & Cantley, L. C. (2006) · Nature · doi:10.1038/nature04869 · Cited by 2,019
“However, it is not clear whether the Raf–ERK pathway is the most critical mediator of Ras-dependent tumorigenesis in all cell types; several other Ras effectors have been identified in the past ten year”
Background
RAS Proteins and Their Regulators in Human Disease
Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943
Self-citation
PI3K and cancer: lessons, challenges and opportunities
Fruman, D. A., & Rommel, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4204 · Cited by 1,762
The emerging mechanisms of isoform-specific PI3K signalling
Vanhaesebroeck, B., Guillermet-Guibert, J., Graupera, M., & Bilanges, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2882 · Cited by 1,767
“, and the Ras family member TC21 (also known as RRAS2) may have a role in the activation of p110”
Background
PI3K in cancer: divergent roles of isoforms, modes of activation and therapeutic targeting
Thorpe, L. M., Yuzugullu, H., & Zhao, J. J. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3860 · Cited by 1,405

See all 327

Authors: Rodriguez-Viciana, P., Sabatier, C., & McCormick, F.
Affiliations: Cancer Research Institute and Comprehensive Cancer Center, University of California
University of California, San Francisco (US)
Corresponding author: McCormick, Frank
ORCID: McCormick, Frank
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2004-06
Volume: 24
Issue: 11
Pages: 4943-4954
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.24.11.4943-4954.2004
PMC: PMC416418
OpenAlex: W2165023373
Cited by: 327
References: 81
Citations by year: 2026: 4 · 2025: 9 · 2024: 16 · 2023: 5 · 2022: 7 · 2021: 12 · 2020: 5 · 2019: 8 · 2018: 18 · 2017: 10 · 2016: 12 · 2015: 12 · 2014: 13 · 2013: 22 · 2012: 24
FWCI: 7.36
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
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 family GTPases, signaling specificity, effector proteins, protein-protein interaction, signaling pathways, cancer
MeSH terms: Humans, Substrate Specificity, Protein Structure, Tertiary, ras Proteins, Phosphatidylinositol 3-Kinases, Proto-Oncogene Proteins c-raf, Protein Isoforms, GTP Phosphohydrolases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Signaling Specificity by Ras Family GTPases Is Determined by the Full Spectrum of Effectors They Regulate

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks