Cited by 348Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysCellular transport and secretion

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Genetic analysis of Ras signalling pathways in cell proliferation, migration and survival

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Drosten, Matthias, Dhawahir, Alma, Sum, Eleanor Y M, Urosevic, Jelena, Lechuga, Carmen G, Esteban, Luis M, Castellano, Esther, Guerra, Carmen, Santos, Eugenio, Barbacid, Mariano·2010·The EMBO Journal

DOI 10.1038/emboj.2010.7PMC PMC2845279

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Abstract

We have used mouse embryonic fibroblasts (MEFs) devoid of Ras proteins to illustrate that they are essential for proliferation and migration, but not for survival, at least in these cells. These properties are unique to the Ras subfamily of proteins because ectopic expression of other Ras-like small GTPases, even when constitutively active, could not compensate for the absence of Ras proteins. Only constitutive activation of components of the Raf/Mek/Erk pathway was sufficient to sustain normal proliferation and migration of MEFs devoid of Ras proteins. Activation of the phosphatidylinositol 3-kinase (PI3K)/PTEN/Akt and Ral guanine exchange factor (RalGEF)/Ral pathways, either alone or in combination, failed to induce proliferation or migration of Rasless cells, although they cooperated with Raf/Mek/Erk signalling to reproduce the full response mediated by Ras signalling. In contrast to current hypotheses, Ras signalling did not induce proliferation by inducing expression of D-type Cyclins. Rasless MEFs had normal levels of Cyclin D1/Cdk4 and Cyclin E/Cdk2. However, these complexes were inactive. Inactivation of the pocket proteins or knock down of pRb relieved MEFs from their dependence on Ras signalling to proliferate.

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Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
Engelman, J. A., Luo, J., & Cantley, L. C. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1879 · Cited by 3,330
Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788
The ErbB signaling network: receptor heterodimerization in development and cancer
Olayioye, M. A., Neve, R. M., Lane, H. A., & Hynes, N. E. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3159 · Cited by 2,489
Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
Diehl, J. A., Cheng, M., Roussel, M. F., & Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.22.3499 · Cited by 2,130
RAS oncogenes: the first 30 years
Malumbres, M., & Barbacid, M. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1097 · Cited by 1,902 · cited 1×
“These studies have illustrated how Ras proteins become activated by growth factor receptors and have unveiled those pathways implicated in mediating downstream signalling to their ultimate effectors (reviewed in Malumbres and Barbacid, 2003).”
BackgroundSelf-citation
Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis
Cully, M., You, H., Levine, A. J., & Mak, T. W. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1819 · Cited by 1,267
The RAF proteins take centre stage
Wellbrock, C., Karasarides, M., & Marais, R. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1498 · Cited by 1,223
Role of Phosphoinositide 3-OH Kinase in Cell Transformation and Control of the Actin Cytoskeleton by Ras
Rodriguez‐Viciana, P., Warne, P. H., Khwaja, A., Marte, B. M., Pappin, D., Das, P., Waterfield, M. D., Ridley, A. J., & Downward, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80226-3 · Cited by 1,060
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 1,011

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Self-citation
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Self-citation
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Souto, E. B., Campos, J. R. S., da Ana, R., Fangueiro, J. F., Martins‐Gomes, C., Durazzo, A., Lucarini, M., Sánchez‐López, E., Espina, M., García, M. L., et al. (2020) · Applied Sciences · doi:10.3390/app10082777 · Cited by 1
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Zeng, T., Jiang, T., Zhang, B., Zhang, T., Dai, W., Yin, X., Li, Y., Wu, C., Wu, Y., Chi, X., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.26.591418 · Cited by 1

Authors: Drosten, M., Dhawahir, A., Sum, E. Y. M., Urosevic, J., Lechuga, C. G., Esteban, L. M., Castellano, E., Guerra, C., Santos, E., & Barbacid, M.
Affiliations: Spanish National Cancer Research Centre (ES)
Universidad de Salamanca (ES)
Corresponding author: Barbacid, Mariano
ORCID: Drosten, Matthias
Urosevic, Jelena
Lechuga, Carmen G
Castellano, Esther
Guerra, Carmen
Santos, Eugenio
Barbacid, Mariano
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2010-02-11
Volume: 29
Issue: 6
Pages: 1091-1104
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/emboj.2010.7
PMC: PMC2845279
OpenAlex: W2113609800
Cited by: 347
References: 60
Citations by year: 2026: 19 · 2025: 24 · 2024: 33 · 2023: 22 · 2022: 35 · 2021: 38 · 2020: 23 · 2019: 13 · 2018: 23 · 2017: 21 · 2016: 11 · 2015: 15 · 2014: 9 · 2013: 17 · 2012: 25
FWCI: 7.81
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
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 › Melanoma and MAPK Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: Ras signaling, Ras proteins, cell proliferation, cell migration, cell survival, mouse embryonic fibroblasts, Raf/MEK/ERK pathway, PI3K/Akt signaling, cyclin D1/CDK4, cyclin E/CDK2, pocket proteins, retinoblastoma protein, cell cycle regulation
MeSH terms: Animals, Cell Movement, Cell Survival, Fibroblasts, Signal Transduction, ras Proteins, Phosphatidylinositol 3-Kinases, Extracellular Signal-Regulated MAP Kinases, raf Kinases, Cell Proliferation, Mice

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Genetic analysis of Ras signalling pathways in cell proliferation, migration and survival

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