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ERK signalling: a master regulator of cell behaviour, life and fate
Abstract
The proteins extracellular signal-regulated kinase 1 (ERK1) and ERK2 are the downstream components of a phosphorelay pathway that conveys growth and mitogenic signals largely channelled by the small RAS GTPases. By phosphorylating widely diverse substrates, ERK proteins govern a variety of evolutionarily conserved cellular processes in metazoans, the dysregulation of which contributes to the cause of distinct human diseases. The mechanisms underlying the regulation of ERK1 and ERK2, their mode of action and their impact on the development and homeostasis of various organisms have been the focus of much attention for nearly three decades. In this Review, we discuss the current understanding of this important class of kinases. We begin with a brief overview of the structure, regulation, substrate recognition and subcellular localization of ERK1 and ERK2. We then systematically discuss how ERK signalling regulates six fundamental cellular processes in response to extracellular cues. These processes are cell proliferation, cell survival, cell growth, cell metabolism, cell migration and cell differentiation.
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“which are associated with a poor prognosis and resistance to certain treatments”
From The Role of KRAS Mutations in Colorectal Cancer: Biological Insights, Clinical Implications, and Future Therapeutic Perspectives (2025) · cites this paper as [12]
In the citing paper
“these mutations promote persistent activation of oncogenic pathways such as MAPK/ERK and PI3K/AKT”
From The Role of KRAS Mutations in Colorectal Cancer: Biological Insights, Clinical Implications, and Future Therapeutic Perspectives (2025) · cites this paper as [12]
In the citing paper
“KRAS mutations in colorectal cancer lead to the sustained activation of critical downstream signaling pathways, including the MAPK/ERK and PI3K/AKT pathways. These pathways promote uncontrolled cell proliferation, inhibit apoptosis, and support tumor growth and metastasis [12].”
From The Role of KRAS Mutations in Colorectal Cancer: Biological Insights, Clinical Implications, and Future Therapeutic Perspectives (2025) · cites this paper as [12]
In the citing paper
“ERK plays important roles in the processes involving cell growth, cell proliferation, and cell survival (Lavoie et al. 2020).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Lavoie et al. 2020
Citations
Cites
Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425
mTOR Signaling in Growth, Metabolism, and Disease
Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555
AMPK: guardian of metabolism and mitochondrial homeostasis
Herzig, S., & Shaw, R. J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.95 · Cited by 4,192
Kim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905
The ground state of embryonic stem cell self-renewal
Ying, Q.-L., Wray, J., Nichols, J., Batlle-Morera, L., Doble, B., Woodgett, J., Cohen, P., & Smith, A. (2008) · Nature · doi:10.1038/nature06968 · Cited by 3,442
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390
Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083
HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., & Denko, N. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.012 · Cited by 2,267
Non-muscle myosin II takes centre stage in cell adhesion and migration
Vicente‐Manzanares, M., Ma, X., Adelstein, R. S., & Horwitz, A. R. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2786 · Cited by 2,137
Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins
Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111
Cell adhesion: integrating cytoskeletal dynamics and cellular tension
Parsons, J. T., Horwitz, A. R., & Schwartz, M. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2957 · Cited by 2,081
FMRP Stalls Ribosomal Translocation on mRNAs Linked to Synaptic Function and Autism
Darnell, J. C., Van Driesche, S. J., Zhang, C., Hung, K. Y. S., Mele, A., Fraser, C. E., Stone, E. F., Chen, C., Fak, J. J., Chi, S. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.013 · Cited by 2,072
Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism
Ying, H., Kimmelman, A. C., Lyssiotis, C. A., Hua, S., Chu, G. C., Fletcher-Sananikone, E., Locasale, J. W., Son, J., Zhang, H., Coloff, J. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.058 · Cited by 2,043
Wise, D. R., DeBerardinis, R. J., Mancuso, A., Sayed, N., Zhang, X.-Y., Pfeiffer, H. K., Nissim, I., Daikhin, E., Yudkoff, M., McMahon, S. B., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810199105 · Cited by 2,001
Glutamine supports pancreatic cancer growth through a KRAS-regulated metabolic pathway
Son, J., Lyssiotis, C. A., Ying, H., Wang, X., Hua, S., Ligorio, M., Perera, R. M., Ferrone, C. R., Mullarky, E., Shyh-Chang, N., et al. (2013) · Nature · doi:10.1038/nature12040 · Cited by 1,990
Bonni, A., Brunet, A., West, A. E., Datta, S. R., Takasu, M. A., & Greenberg, M. E. (1999) · Science · doi:10.1126/science.286.5443.1358 · Cited by 1,908
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876
Chen, L., Willis, S. N., Wei, A., Smith, B. J., Fletcher, J. I., Hinds, M. G., Colman, P. M., Day, C. L., Adams, J. M., & Huang, D. C. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.030 · Cited by 1,816
BCL-2 family proteins: changing partners in the dance towards death
Kale, J., Osterlund, E. J., & Andrews, D. W. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.186 · Cited by 1,574
Control of cell cycle transcription during G1 and S phases
Bertoli, C., Skotheim, J. M., & de Bruin, R. A. M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3629 · Cited by 1,567
Multiple Ras-dependent phosphorylation pathways regulate Myc protein stabilityPreprint
Sears, R. C., Nuckolls, F., Haura, E. B., Taya, Y., Tamai, K., & Nevins, J. R. (2000) · Genes & Development · doi:10.1101/gad.836800 · Cited by 1,411
FAK–Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
Webb, D. J., Donais, K., Whitmore, L. A., Thomas, S. Μ., Turner, C. E., Parsons, J. T., & Horwitz, A. F. (2004) · Nature Cell Biology · doi:10.1038/ncb1094 · Cited by 1,387
Phosphorylation and Functional Inactivation of TSC2 by Erk
Ma, L., Chen, Z., Erdjument-Bromage, H., Tempst, P., & Pandolfi, P. P. (2005) · Cell · doi:10.1016/j.cell.2005.02.031 · Cited by 1,268
Oncogene ablation-resistant pancreatic cancer cells depend on mitochondrial function
Viale, A., Pettazzoni, P., Lyssiotis, C. A., Ying, H., Sánchez, N., Marchesini, M., Carugo, A., Green, T., Seth, S., Giuliani, V., et al. (2014) · Nature · doi:10.1038/nature13611 · Cited by 1,259
Regulation of Cell Motility by Mitogen-activated Protein Kinase
Klemke, R. L., Cai, S., Giannini, A. L. M., Gallagher, P. J., de Lanerolle, P., & Cheresh, D. A. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.2.481 · Cited by 1,239
Cyclin D1 Expression Is Regulated Positively by the p42/p44 and Negatively by the p38/HOG Pathway
Lavoie, J. N., L’Allemain, G., Brunet, A., Müller, R., & Pouysségur, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20608 · Cited by 1,210
c-Myc transactivation of LDH-A : Implications for tumor metabolism and growth
Shim, H., Dolde, C., Lewis, B. C., Wu, C.-S., Dang, G., Jungmann, R. A., Dalla-Favera, R., & Dang, C. V. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6658 · Cited by 1,092
The MAPK cascade is required for mammalian associative learning
Atkins, C. M., Selcher, J. C., Petraitis, J. J., Trzaskos, J. M., & Sweatt, J. D. (1998) · Nature Neuroscience · doi:10.1038/2836 · Cited by 1,083
Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARFPreprint
Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,069
Metabolic requirements for the maintenance of self-renewing stem cells
Ito, K., & Suda, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3772 · Cited by 1,014
Linking actin dynamics and gene transcription to drive cellular motile functions
Olson, E. N., & Nordheim, A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2890 · Cited by 958
Frederick, D. T., Piris, A., Cogdill, A. P., Cooper, Z. A., Lezcano, C., Ferrone, C. R., Mitra, D., Boni, A., Newton, L. P., Liu, C., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-1630 · Cited by 944
Protein kinases: evolution of dynamic regulatory proteins
Taylor, S. S., & Kornev, A. P. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.006 · Cited by 940
Molecular interpretation of ERK signal duration by immediate early gene products
Murphy, L. O., Smith, S. W., Chen, R., Fingar, D. C., & Blenis, J. (2002) · Nature Cell Biology · doi:10.1038/ncb822 · Cited by 928
ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect
Yang, W., Zheng, Y., Xia, Y., Ji, H., Chen, X., Guo, F., Lyssiotis, C. A., Aldape, K., Cantley, L. C., & Lu, Z. (2012) · Nature Cell Biology · doi:10.1038/ncb2629 · Cited by 926
Jones, M. W., Errington, M. L., French, P. J., Fine, A., Bliss, T., Garel, S., Charnay, P., Bozon, B., Laroche, S., & Davis, S. (2001) · Nature Neuroscience · doi:10.1038/85138 · Cited by 925
Rauen, K. A. (2013) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-091212-153523 · Cited by 908
Opposing BMP and EGF signalling pathways converge on the TGF-β family mediator Smad1
Kretzschmar, M., Doody, J. F., & Massagué, J. (1997) · Nature · doi:10.1038/39348 · Cited by 878
Deregulation of Glucose Transporter 1 and Glycolytic Gene Expression by c-Myc
Osthus, R. C., Shim, H., Kim, S., Li, Q., Reddy, R., Mukherjee, M., Xu, Y., Wonsey, D. R., Lee, L. A., & Dang, C. V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000023200 · Cited by 876
Oncogenic BRAF Regulates Oxidative Metabolism via PGC1α and MITF
Haq, R., Shoag, J., Andreu-Perez, P., Yokoyama, S., Edelman, H., Rowe, G. C., Frederick, D. T., Hurley, A. D., Nellore, A., Kung, A. L., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.003 · Cited by 818
Kunath, T., Saba-El-Leil, M. K., Almosailleakh, M., Wray, J. P., Meloche, S., & Smith, A. G. (2007) · Development · doi:10.1242/dev.02880 · Cited by 814
Transforming p21 Mutants and c-Ets-2 Activate the Cyclin D1 Promoter through Distinguishable Regions
Albanese, C., Johnson, J., Watanabe, G., Eklund, N., Vu, D., Arnold, A., & Pestell, R. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23589 · Cited by 802
Richard, D. E., Berra, E., Gothié, E., Roux, D., & Pouysségur, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.32631 · Cited by 797
Yeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791
Roux, P. P., Ballif, B. A., Anjum, R., Gygi, S. P., & Blenis, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405659101 · Cited by 750
ERK implication in cell cycle regulation
Chambard, J., LeFloch, R., Pouysségur, J., & Lenormand, P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.11.010 · Cited by 749
S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth
Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729
High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
Schödel, J., Oikonomopoulos, S., Ragoussis, J., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R. (2011) · Blood · doi:10.1182/blood-2010-10-314427 · Cited by 724
ERK promotes tumorigenesis by inhibiting FOXO3a via MDM2-mediated degradation
Yang, J.-Y., Zong, C. S., Xia, W., Yamaguchi, H., Ding, Q., Xie, X., Lang, J.-Y., Lai, C., Chang, C. J., Huang, W., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1676 · Cited by 720
Gain-of-function RAF1 mutations cause Noonan and LEOPARD syndromes with hypertrophic cardiomyopathy
Pandit, B., Sárközy, A., Pennacchio, L. A., Carta, C., Oishi, K., Martinelli, S., Pogna, E. A., Schackwitz, W., Ustaszewska, A., Landstrom, A. P., et al. (2007) · Nature Genetics · doi:10.1038/ng2073 · Cited by 715
Vazquez, F., Lim, J.-H., Chim, H., Bhalla, K., Girnun, G., Pierce, K., Clish, C. B., Granter, S. R., Widlund, H. R., Spiegelman, B. M., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2012.11.020 · Cited by 715
An Insulin-Stimulated Protein Kinase Similar to Yeast Kinases Involved in Cell Cycle Control
Boulton, T. G., Yancopoulos, G. D., Gregory, J. S., Slaughter, C. A., Moomaw, C. R., Hsu, J., & Cobb, M. H. (1990) · Science · doi:10.1126/science.2164259 · Cited by 707
Regulation of RAF protein kinases in ERK signalling
Lavoie, H., & Therrien, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3979 · Cited by 702
Self-citationErk2 Phosphorylation of Drp1 Promotes Mitochondrial Fission and MAPK-Driven Tumor Growth
Kashatus, J. A., Nascimento, A., Myers, L. J., Sher, A., Byrne, F. L., Hoehn, K. L., Counter, C. M., & Kashatus, D. F. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.002 · Cited by 691
Patient-specific induced pluripotent stem-cell-derived models of LEOPARD syndrome
Carvajal-Vergara, X., Sevilla, A., D’Souza, S. L., Ang, Y.-S., Schaniel, C., Lee, D.-F., Yang, L., Kaplan, A. D., Adler, E. D., Rozov, R., et al. (2010) · Nature · doi:10.1038/nature09005 · Cited by 690
Zalfa, F., Giorgi, M., Primerano, B., Moro, A., Di Penta, A., Reis, S., Oostra, B., & Bagni, C. (2003) · Cell · doi:10.1016/s0092-8674(03)00079-5 · Cited by 676
c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I
Grandori, C., Gomez-Roman, N., Felton-Edkins, Z. A., Ngouenet, C., Galloway, D. A., Eisenman, R. N., & White, R. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1224 · Cited by 659
Kim, J.-W., Gao, P., Liu, Y.-C., Semenza, G. L., & Dang, C. V. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00440-07 · Cited by 658
Keap1 loss promotes Kras-driven lung cancer and results in dependence on glutaminolysis
Romero, R., Sayin, V. I., Davidson, S. M., Bauer, M. R., Singh, S. X., LeBoeuf, S. E., Karakousi, T. R., Ellis, D. C., Bhutkar, A., Sánchez-Rivera, F. J., et al. (2017) · Nature Medicine · doi:10.1038/nm.4407 · Cited by 652
Drosophila myc Regulates Cellular Growth during Development
Johnston, L. A., Prober, D. A., Edgar, B. A., Eisenman, R. N., & Gallant, P. (1999) · Cell · doi:10.1016/s0092-8674(00)81512-3 · Cited by 648
Mouse development and cell proliferation in the absence of D-cyclins
Kozar, K., Ciemerych, M. A., Rebel, V. I., Shigematsu, H., Zagozdzon, A., Sicinska, E., Geng, Y., Yu, Q., Bhattacharya, S., Bronson, R. T., et al. (2004) · Cell · doi:10.1016/j.cell.2004.07.025 · Cited by 647
BCL-2 proteins and apoptosis: Recent insights and unknowns
Edlich, F. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.190 · Cited by 640
MAP kinase links the transcription factor Microphthalmia to c-Kit signalling in melanocytes
Hemesath, T. J., Price, E. R., Takemoto, C. M., Badalian, T. M., & Fisher, D. E. (1998) · Nature · doi:10.1038/34681 · Cited by 631
Chung, J., Uchida, E., Grammer, T. C., & Blenis, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6508 · Cited by 620
Austin, S., & St‐Pierre, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.113662 · Cited by 617
The Fragile X Syndrome Protein Represses Activity-Dependent Translation through CYFIP1, a New 4E-BP
Napoli, I., Mercaldo, V., Boyl, P. P., Eleuteri, B., Zalfa, F., De Rubeis, S., Di Marino, D., Mohr, E., Massimi, M., Falconi, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.031 · Cited by 609
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
Ray, L. B., & Sturgill, T. W. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.6.1502 · Cited by 592
Suppression of SHP-2 and ERK Signalling Promotes Self-Renewal of Mouse Embryonic Stem Cells
Burdon, T., Stracey, C., Chambers, I., Nichols, J., & Smith, A. G. (1999) · Developmental Biology · doi:10.1006/dbio.1999.9265 · Cited by 585
Lee, B., Thirunavukkarasu, K., Zhou, L., Pastore, L., Baldini, A., Hecht, J. T., Geoffrey, V., Ducy, P. F., & Karsenty, G. (1997) · Nature Genetics · doi:10.1038/ng0797-307 · Cited by 567
Negative feedback regulation of the ERK1/2 MAPK pathway
Lake, D., Corrêa, S. A. L., & Müller, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2297-8 · Cited by 565
Activation of ternary complex factor Elk‐1 by MAP kinases.
Janknecht, R., Ernst, W. H., Pingoud, V., & Nordheim, A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06204.x · Cited by 561
Mutations in CIC and FUBP1 Contribute to Human Oligodendroglioma
Bettegowda, C., Agrawal, N., Jiao, Y., Sausen, M., Wood, L. D., Hruban, R. H., Rodríguez, F. J., Cahill, D. P., McLendon, R. E., Riggins, G. J., et al. (2011) · Science · doi:10.1126/science.1210557 · Cited by 561
Integrating Patterning Signals: Wnt/GSK3 Regulates the Duration of the BMP/Smad1 Signal
Fuentealba, L. C., Eivers, E., Ikeda, A., Hurtado, C., Kuroda, H., Pera, E. M., & Robertis, E. M. D. (2007) · Cell · doi:10.1016/j.cell.2007.09.027 · Cited by 555
MAPK Pathways Activate and Phosphorylate the Osteoblast-specific Transcription Factor, Cbfa1
Xiao, G., Jiang, D., Thomas, P. E., Benson, M. D., Guan, K., Karsenty, G., & Franceschi, R. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4453 · Cited by 552
Wu, M., Hemesath, T. J., Takemoto, C. M., Horstmann, M. A., Wells, A. G., Price, E. R., Fisher, D. Z., & Fisher, D. E. (2000) · Genes & Development · doi:10.1101/gad.14.3.301 · Cited by 548
eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression
Furic, L., Rong, L., Larsson, O. S., Koumakpayi, I. H., Yoshida, K., Brueschke, A., Petroulakis, E., Robichaud, N., Pollak, M., Gaboury, L. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005320107 · Cited by 541
Rho GTPase signaling complexes in cell migration and invasion
Lawson, C. D., & Ridley, A. J. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201612069 · Cited by 539
The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity
Shahbazian, D., Roux, P. P., Mieulet, V., Cohen, M. S., Raught, B., Taunton, J., Hershey, J. W. B., Blenis, J., Pende, M., & Sonenberg, N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601166 · Cited by 532
Case, L. B., & Waterman, C. M. (2015) · Nature Cell Biology · doi:10.1038/ncb3191 · Cited by 520
PKM2, cancer metabolism, and the road ahead
Dayton, T. L., Jacks, T., & Vander Heiden, M. G. (2016) · The EMBO Reports · doi:10.15252/embr.201643300 · Cited by 515
Minoux, M., & Rijli, F. M. (2010) · Development · doi:10.1242/dev.040048 · Cited by 507
Ueda, T., Watanabe-Fukunaga, R., Fukuyama, H., Nagata, S., & Fukunaga, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.15.6539-6549.2004 · Cited by 507
Frequency-Modulated Pulses of ERK Activity Transmit Quantitative Proliferation Signals
Albeck, J. G., Mills, G. B., & Brugge, J. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.002 · Cited by 494
Oncogenic K‐Ras decouples glucose and glutamine metabolism to support cancer cell growth
Gaglio, D., Metallo, C. M., Gameiro, P. A., Hiller, K., Danna, L. S., Balestrieri, C., Alberghina, L., Stephanopoulos, G., & Chiaradonna, F. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.56 · Cited by 492
Genomic and biochemical insights into the specificity of ETS transcription factors
Hollenhorst, P. C., McIntosh, L. P., & Graves, B. J. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.79.081507.103945 · Cited by 490
A role for the Ras signalling pathway in synaptic transmission and long-term memory
Brambilla, R., Gnesutta, N., Minichiello, L., White, G., Roylance, A. J., Herron, C. E., Ramsey, M., Wolfer, D. P., Cestari, V., Rossi‐Arnaud, C., et al. (1997) · Nature · doi:10.1038/36849 · Cited by 474
Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK
Allan, L. A., MORRICE, N. A., Brady, S. C., Magee, G. J., Pathak, S., & Clarke, P. R. (2003) · Nature Cell Biology · doi:10.1038/ncb1005 · Cited by 474
c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription
Arabi, A., Wu, S., Ridderstråle, K., Bierhoff, H., Shiue, C.-N., Fátyol, K., Fahlén, S., Hydbring, P., Söderberg, O., Grummt, I., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1225 · Cited by 471
Kawamura-Saito, M., Yamazaki, Y., Kaneko, K., Kawaguchi, N., Kanda, H., Mukai, H., Gotoh, T., Motoi, T., Fukayama, M., Aburatani, H., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl136 · Cited by 467
On being the right (cell) size
Ginzberg, M. B., Kafri, R., & Kirschner, M. W. (2015) · Science · doi:10.1126/science.1245075 · Cited by 445
Wiggin, G. R., Soloaga, A., Foster, J. M., Murray-Tait, V., Cohen, P., & Arthur, J. S. C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2871-2881.2002 · Cited by 445
Neurofibromin Regulation of ERK Signaling Modulates GABA Release and Learning
Cui, Y., Costa, R. M., Murphy, G. G., Elgersma, Y., Zhu, Y., Gutmann, D. H., Parada, L. F., Módy, I., & Silva, A. J. (2008) · Cell · doi:10.1016/j.cell.2008.09.060 · Cited by 445
The Nature of Embryonic Stem Cells
Martello, G., & Smith, A. G. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013116 · Cited by 444
The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
King, A. J., Sun, H., Diaz, B., Barnard, D., Miao, W., Bagrodia, S., & Marshall, M. S. (1998) · Nature · doi:10.1038/24184 · Cited by 443
Qi, X., Li, T.-G., Hao, J., Hu, J., Wang, J., Simmons, H., Miura, S., Mishina, Y. M., & Zhao, G.-Q. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401367101 · Cited by 440
Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439
Balancing BMP Signaling through Integrated Inputs into the Smad1 Linker
Sapkota, G. P., Alarcón, C. R., Spagnoli, F. M., Brivanlou, A. H., & Massagué, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.006 · Cited by 419
Serasinghe, M. N., Wieder, S. Y., Renault, T. T., Elkholi, R., Asciolla, J. J., Yao, J. L., Jabado, O., Hoehn, K. L., Kageyama, Y., Sesaki, H., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.003 · Cited by 400
Hu, S., Xie, Z., Onishi, A., Yu, X., Jiang, L., Lin, J., Rho, H., Woodard, C. L., Wang, H., Jeong, J. S., et al. (2009) · Cell · doi:10.1016/j.cell.2009.08.037 · Cited by 390
Myc-dependent regulation of ribosomal RNA synthesis during Drosophila development
Grewal, S., Li, L., Orian, A., Eisenman, R. N., & Edgar, B. A. (2005) · Nature Cell Biology · doi:10.1038/ncb1223 · Cited by 387
Four Key Steps Control Glycolytic Flux in Mammalian Cells
Tanner, L. B., Goglia, A. G., Wei, M. H., Sehgal, T., Parsons, L. R., Park, J. O., White, E., Toettcher, J. E., & Rabinowitz, J. D. (2018) · Cell Systems · doi:10.1016/j.cels.2018.06.003 · Cited by 383
Transformation of NIH 3T3 cells by microinjection of Ha-ras p21 protein
Stacey, D. W., & Kung, H. (1984) · Nature · doi:10.1038/310508a0 · Cited by 380
Esnault, C., Stewart, A., Gualdrini, F., East, P., Horswell, S. D., Matthews, N., & Treisman, R. (2014) · Genes & Development · doi:10.1101/gad.239327.114 · Cited by 370
Targeting the eIF4F Translation Initiation Complex: A Critical Nexus for Cancer Development
Pelletier, J., Graff, J., Ruggero, D., & Sonenberg, N. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2789 · Cited by 367
c-Myc enhances protein synthesis and cell size during B lymphocyte development
Iritani, B. M., & Eisenman, R. N. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13180 · Cited by 364
Zheng, B., Jeong, J. H., Asara, J. M., Yuan, Y.-Y., Granter, S. R., Chin, L., & Cantley, L. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.026 · Cited by 364
Emerging roles of ATF2 and the dynamic AP1 network in cancer
Lopez‐Bergami, P., Lau, E. K., & Ronai, Z. A. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2681 · Cited by 353
Oncogenic MAPK Signaling Stimulates mTORC1 Activity by Promoting RSK-Mediated Raptor Phosphorylation
Carrière, A., Cargnello, M., Julien, L.-A., Gao, H., Bonneil, É., Thibault, P., & Roux, P. P. (2008) · Current Biology · doi:10.1016/j.cub.2008.07.078 · Cited by 348
Genetic analysis of Ras signalling pathways in cell proliferation, migration and survival
Drosten, M., Dhawahir, A., Sum, E. Y. M., Urosevic, J., Lechuga, C. G., Esteban, L. M., Castellano, E., Guerra, C., Santos, E., & Barbacid, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.7 · Cited by 347
Transcriptional regulation of the cyclin D1 gene at a glance
Klein, E. A., & Assoian, R. K. (2008) · Journal of Cell Science · doi:10.1242/jcs.039131 · Cited by 341
Murphy, L. O., MacKeigan, J. P., & Blenis, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.144-153.2004 · Cited by 339
Fincham, V. J., James, M., Frame, M. C., & Winder, S. J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.12.2911 · Cited by 337
The transcriptional and signalling networks of pluripotency
Ng, H., & Surani, M. A. (2011) · Nature Cell Biology · doi:10.1038/ncb0511-490 · Cited by 334
Comparative Metabolic Flux Profiling of Melanoma Cell Lines
Scott, D. A., Richardson, A. D., Filipp, F. V., Knutzen, C. A., Chiang, G. G., Ronai, Z. A., Osterman, A. L., & Smith, J. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.282046 · Cited by 328
Domina, A. M., Vrana, J. A., Gregory, M. A., Hann, S. R., & Craig, R. W. (2004) · Oncogene · doi:10.1038/sj.onc.1207692 · Cited by 327
PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase
Formstecher, É., Ramos, J. W., Fauquet, M., Calderwood, D., Hsieh, J.-C., Canton, B., Nguyen, X.-T., Barnier, J., Camonis, J., Ginsberg, M. H., et al. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00035-1 · Cited by 320
Bozon, B., Davis, S., & Laroche, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00674-3 · Cited by 317
Mutant Kras copy number defines metabolic reprogramming and therapeutic susceptibilities
Kerr, E. M., Gaude, E., Turrell, F. K., Frezza, C., & Martins, C. P. (2016) · Nature · doi:10.1038/nature16967 · Cited by 316
ERK1 and ERK2 Map Kinases: Specific Roles or Functional Redundancy?
Buscà, R., Pouysségur, J., & Lenormand, P. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00053 · Cited by 303
Molecular basis of MAP kinase regulation
Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302
Nayal, A., Webb, D. J., Brown, C. M., SCHAEFER, E. M., Vicente‐Manzanares, M., & Horwitz, A. R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200509075 · Cited by 302
Rsk1 mediates a MEK–MAP kinase cell survival signal
Shimamura, A., Ballif, B. A., Richards, S. A., & Blenis, J. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00310-9 · Cited by 296
Martı́nez-Quiles, N., Ho, H. H., Kirschner, M. W., Ramesh, N., & Geha, R. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5269-5280.2004 · Cited by 296
Chen, R., Abate, C., & Blenis, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10952 · Cited by 294
Propagating Wave of ERK Activation Orients Collective Cell Migration
Aoki, K., Kondo, Y., Naoki, H., Hiratsuka, T., Itoh, R. E., & Matsuda, M. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.10.016 · Cited by 292
Parmenter, T. J., Kleinschmidt, M., Kinross, K. M., Bond, S. T., Li, J., Kaadige, M. R., Rao, A. D., Sheppard, K. E., Hugo, W., Pupo, G. M., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0440 · Cited by 291
Prieto, J., León, M., Ponsoda, X., Sendra, R., Bort, R., Ferrer‐Lorente, R., Raya, Á., López‐García, C., & Torres, J. (2016) · Nature Communications · doi:10.1038/ncomms11124 · Cited by 285
PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK activation
Slack‐Davis, J. K., Eblen, S. T., Zečević, M., Boerner, S. A., Tarcsafalvi, A., Diaz, H. B., Marshall, M. S., Weber, M. J., Parsons, J. T., & Catling, A. D. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212141 · Cited by 283
Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry
Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00161-3 · Cited by 282
ETS gene fusions in prostate cancer
Clark, J. P., & Cooper, C. S. (2009) · Nature Reviews Urology · doi:10.1038/nrurol.2009.127 · Cited by 277
Liang, Q., Wiese, R. J., Bueno, O. F., Dai, Y., Markham, B. E., & Molkentin, J. D. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.21.7460-7469.2001 · Cited by 271
Adachi, M., Fukuda, M., & Nishida, E. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5347 · Cited by 268
ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)
Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268
Mylonis, I., Chachami, G., Samiotaki, M. K., Panayotou, G., Paraskeva, E., Kalousi, A., Georgatsou, E., Bonanou, S., & Simos, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605058200 · Cited by 266
MYC Oncogene Contributions to Release of Cell Cycle Brakes
García-Gutiérrez, L., Delgado, M. D., & León, J. (2019) · Genes · doi:10.3390/genes10030244 · Cited by 264
Growth-factor-dependent mitogenesis requires two distinct phases of signalling
Jones, S. M., & Kazlauskas, A. (2001) · Nature Cell Biology · doi:10.1038/35055073 · Cited by 263
Regulation of Primary Response Genes
Fowler, T., Sen, R., & Roy, A. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.014 · Cited by 262
Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259
Rivera, V. M., Miranti, C. K., Misra, R., Ginty, D. D., Chen, R. H., Blenis, J., & Greenberg, M. E. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6260 · Cited by 258
Berra, E., Díaz-Meco, M. T., & Moscat, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10792 · Cited by 255
Fos Family Members Induce Cell Cycle Entry by Activating Cyclin D1
Brown, J. R., Nigh, E. A., Lee, R. J., Ye, H., Thompson, M. A., Saudou, F., Pestell, R. G., & Greenberg, M. E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5609 · Cited by 253
Sheikh, F., Raskin, A., Chu, P., Lange, S., Domenighetti, A. A., Zheng, M., Liang, X., Zhang, T., Yajima, T., Gu, Y., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34472 · Cited by 252
Oncogenic KRAS supports pancreatic cancer through regulation of nucleotide synthesis
Santana-Codina, N., Roeth, A. A., Zhang, Y., Yang, A., Mashadova, O., Asara, J. M., Wang, X., Bronson, R. T., Lyssiotis, C. A., Ying, H., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07472-8 · Cited by 252
Ras trafficking, localization and compartmentalized signalling
Prior, I. A., & Hancock, J. F. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.09.002 · Cited by 242
Stefanovsky, V. Y., Pelletier, G., Hannan, R. D., Gagnon-Kugler, T., Rothblum, L. I., & Moss, T. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00384-7 · Cited by 242
Ishibe, S., Joly, D., Liu, Z., & Cantley, L. G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.006 · Cited by 241
Ligand-Specific c-Fos Expression Emerges from the Spatiotemporal Control of ErbB Network Dynamics
Nakakuki, T., Birtwistle, M. R., Saeki, Y., Yumoto, N., Ide, K., Nagashima, T., Brusch, L., Ogunnaike, B. A., Okada, M., & Kholodenko, B. Ν. (2010) · Cell · doi:10.1016/j.cell.2010.03.054 · Cited by 241
Ge, C., Xiao, G., Jiang, D., Yang, Q., Hatch, N. E., Roca, H., & Franceschi, R. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040980 · Cited by 237
Hoshi, M. M., Nishida, E., & Sakai, H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60730-6 · Cited by 235
Wellbrock, C., & Arozarena, I. (2015) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12370 · Cited by 233
Regulation of carbamoyl phosphate synthetase by MAP kinase
Graves, L. M., Guy, H. I., Kozlowski, P., Huang, M., Lazarowski, E. R., Pope, R. M., Collins, M. A., Dahlstrand, E. N., Earp, H. S., & Evans, D. R. (2000) · Nature · doi:10.1038/35002111 · Cited by 232
Hiratsuka, T., Fujita, Y., Naoki, H., Aoki, K., Kamioka, Y., & Matsuda, M. (2015) · eLife · doi:10.7554/elife.05178 · Cited by 230
Multisite Phosphorylation Regulates Bim Stability and Apoptotic Activity
Hübner, A., Barrett, T., Flavell, R. A., & Davis, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.025 · Cited by 228
Crews, C. M., & Erikson, R. L. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.17.8205 · Cited by 226
Sengupta, T. K., Talbot, E. S., Scherle, P., & Ivashkiv, L. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11107 · Cited by 226
Plasticity of Cell Migration In Vivo and In Silico
Boekhorst, V. T., Preziosi, L., & Friedl, P. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125201 · Cited by 225
Dysregulation of the basal RNA polymerase transcription apparatus in cancer
Bywater, M. J., Pearson, R. B., McArthur, G. A., & Hannan, R. D. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3496 · Cited by 224
A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy
Lorenz, K., Schmitt, J. P., Schmitteckert, E. M., & Lohse, M. J. (2008) · Nature Medicine · doi:10.1038/nm.1893 · Cited by 221
Stefanovsky, V. Y., Langlois, F., Gagnon-Kugler, T., Rothblum, L. I., & Moss, T. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.023 · Cited by 220
Adachi, M., Fukuda, M., & Nishida, E. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.849 · Cited by 218
Ishibe, S., Joly, D., Zhu, X., & Cantley, L. G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00406-4 · Cited by 218
Cardio-Facio-Cutaneous Syndrome: Clinical Features, Diagnosis, and Management Guidelines
Pierpont, M. E., Magoulas, P. L., Adi, S., Kavamura, M. I., Neri, G., Noonan, J. A., Pierpont, E. I., Reinker, K. A., Roberts, A. E., Shankar, S. P., et al. (2014) · PEDIATRICS · doi:10.1542/peds.2013-3189 · Cited by 217
A PGC1α-mediated transcriptional axis suppresses melanoma metastasis
Luo, C., Lim, J.-H., Lee, Y., Granter, S. R., Thomas, A., Vázquez, F., Widlund, H. R., & Puigserver, P. (2016) · Nature · doi:10.1038/nature19347 · Cited by 213
Competing memories of mitogen and p53 signalling control cell-cycle entry
Yang, H. W., Chung, M., Kudo, T., & Meyer, T. (2017) · Nature · doi:10.1038/nature23880 · Cited by 211
Fujita, N., Sato, S., & Tsuruo, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306614200 · Cited by 210
Ueda, T., Sasaki, M., Elia, A., Chio, I. I. C., Hamada, K., Fukunaga, R., & Mak, T. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008136107 · Cited by 209
Shukla, V., Coumoul, X., Wang, R.-H., Kim, H., & Deng, C. (2007) · Nature Genetics · doi:10.1038/ng2096 · Cited by 203
MAD1 and c‐MYC regulate UBF and rDNA transcription during granulocyte differentiation
Poortinga, G., Hannan, K., Snelling, H., Walkley, C. R., Jenkins, A., Sharkey, K., Wall, M., Brandenburger, Y., Palatsides, M., Pearson, R., et al. (2004) · EMBO Journal · doi:10.1038/sj.emboj.7600335 · Cited by 198
Good, M. C., Tang, G. Y., Singleton, J., Reményi, A., & Lim, W. A. (2009) · Cell · doi:10.1016/j.cell.2009.01.049 · Cited by 197
Hall, A., Meyle, K. D., Lange, M. K., Klima, M., Sanderhoff, M., Dahl, C., Abildgaard, C., Thorup, K., Moghimi, S. M., Jensen, P. B., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.965 · Cited by 191
ERKs in cancer: friends or foes?
Deschênes-Simard, X., Kottakis, F., Meloche, S., & Ferbeyre, G. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-2381 · Cited by 186
Ünal, E. B., Uhlitz, F., & Blüthgen, N. (2017) · FEBS Letters · doi:10.1002/1873-3468.12740 · Cited by 182
ERK1 and ERK2 regulate embryonic stem cell self-renewal through phosphorylation of Klf4
Kim, M. O., Kim, S.-H., Cho, Y., Nadas, J., Jeong, C., Yao, K., Kim, D. J., Yu, D.-H., Keum, Y.-S., Lee, K.-Y., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2217 · Cited by 179
Ribosomal S6 Kinase (RSK) Regulates Phosphorylation of Filamin A on an Important Regulatory Site
Woo, M. S., Ohta, Y., Rabinovitz, I., Stossel, T. P., & Blenis, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.3025-3035.2004 · Cited by 179
ERK1/2‐dependent phosphorylation of BimEL promotes its rapid dissociation from Mcl‐1 and Bcl‐xL
Ewings, K. E., Hadfield‐Moorhouse, K., Wiggins, C. M., Wickenden, J. A., Balmanno, K., Gilley, R., Degenhardt, K., White, E., & Cook, S. J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601723 · Cited by 176
Zheng, Y., Xia, Y., Hawke, D. H., Hallé, M., Tremblay, M. L., Gao, X., Zhou, X. Z., Aldape, K., Cobb, M. H., Xie, K., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.013 · Cited by 174
Twigg, S. R. F., Vorgia, E., McGowan, S. J., Peraki, I., Fenwick, A. L., Sharma, V., Allégra, M., Ζαραγκούλιας, Α., Akha, E. S., Knight, S. J. L., et al. (2013) · Nature Genetics · doi:10.1038/ng.2539 · Cited by 173
Newbern, J., Zhong, J., Wickramasinghe, R. S., Li, X., Wu, Y., Samuels, I., Cherosky, N., Karlo, J. C., O'Loughlin, B., Wikenheiser, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805239105 · Cited by 172
Addiction to Coupling of the Warburg Effect with Glutamine Catabolism in Cancer Cells
Smith, B., Schafer, X., Ambeskovic, A., Spencer, C. M., Land, H., & Munger, J. C. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.045 · Cited by 172
ERK signalling as a regulator of cell motility
Tanimura, S., & Takeda, K. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx048 · Cited by 172
Sgouras, D. N., Athanasiou, M., Beal, G., Fisher, R. J., Blair, D. G., & Mavrothalassitis, G. J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00160.x · Cited by 171
ERK-MAPK Drives Lamellipodia Protrusion by Activating the WAVE2 Regulatory Complex
Mendoza, M. C., Er, E. E., Zhang, W., Ballif, B. A., Elliott, H. L., Danuser, G., & Blenis, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.031 · Cited by 169
Ye, Q., Cai, W., Zheng, Y., Evers, B. M., & She, Q. (2013) · Oncogene · doi:10.1038/onc.2013.122 · Cited by 168
Li, Z., Fei, T., Zhang, J., Zhu, G., Wang, L., Lu, D., Chi, X., Teng, Y., Hou, N., Yang, X. Y., et al. (2012) · Cell stem cell · doi:10.1016/j.stem.2011.12.016 · Cited by 168
STAT3 Phosphorylation at Tyrosine 705 and Serine 727 Differentially Regulates Mouse ESC Fates
Huang, G., Yan, H., Ye, S., Tong, C., & Ying, Q. (2013) · Stem Cells · doi:10.1002/stem.1609 · Cited by 165
Tee, W.-W., Shen, S. S., Oksuz, O., Narendra, V., & Reinberg, D. (2014) · Cell · doi:10.1016/j.cell.2014.01.009 · Cited by 165
Kosako, H., Yamaguchi, N., Aranami, C., Ushiyama, M., Kose, S., Imamoto, N., Taniguchi, H., Nishida, E., & Hattori, S. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1656 · Cited by 162
SRF Co-factors Control the Balance between Cell Proliferation and Contractility
Gualdrini, F., Esnault, C., Horswell, S., Stewart, A., Matthews, N., & Treisman, R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.10.016 · Cited by 161
Oncogenic ETS proteins mimic activated RAS/MAPK signaling in prostate cellsPreprint
Hollenhorst, P. C., Ferris, M. W., Hull, M. A., Chae, H., Kim, S., & Graves, B. J. (2011) · Genes & Development · doi:10.1101/gad.17546311 · Cited by 155
Small Molecule Inhibition of ERK Dimerization Prevents Tumorigenesis by RAS-ERK Pathway Oncogenes
Herrero, A., Pinto, A., Colón‐Bolea, P., Casar, B., Jones, M., Agudo‐Ibáñez, L., Vidal, R., Tenbaum, S. P., Nuciforo, P. G., Valdizán, E. M., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.07.001 · Cited by 154
Subcellular Localization Determines MAP Kinase Signal Output
Harding, A. S., Tian, T., Westbury, E., Frische, E. W., & Hancock, J. F. (2005) · Current Biology · doi:10.1016/j.cub.2005.04.020 · Cited by 153
Cancer mutations and targeted drugs can disrupt dynamic signal encoding by the Ras-Erk pathway
Bugaj, L. J., Sabnis, A. J., Mitchell, A., Garbarino, J. E., Toettcher, J. E., Bivona, T. G., & Lim, W. A. (2018) · Science · doi:10.1126/science.aao3048 · Cited by 153
Casar, B., Pinto, A., & Crespo, P. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.024 · Cited by 152
MEK drives BRAF activation through allosteric control of KSR proteins
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Metadata
- Authors
- Lavoie, H., Gagnon, J., & Therrien, M.
- Affiliations
- Institute for Research in Immunology and Cancer (CA)
- Corresponding author
- Therrien, Marc
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2020-06-23
- Volume
- 21
- Issue
- 10
- Pages
- 607-632
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W3036759197
- Cited by
- 1,185
- References
- 295
- Citations by year
- 2026: 195 · 2025: 253 · 2024: 248 · 2023: 208 · 2022: 163 · 2021: 110 · 2020: 7
- FWCI
- 11.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (FDN 388023)
- 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 › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- ERK1, ERK2, MAPK signaling, Ras GTPase, kinase regulation, substrate recognition, subcellular localization, cell proliferation, cell survival, cell growth, cellular metabolism, cell migration, cell differentiation, disease
- MeSH terms
- Animals, Cell Differentiation, Cell Movement, Humans, Signal Transduction, Extracellular Signal-Regulated MAP Kinases, Cell Proliferation
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