The DOI matches its Crossref record; 295 of the 295 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“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
Items 201–295 of 295
Panja, D., Kenney, J. W., D’Andrea, L., Zalfa, F., Vedeler, A., Wibrand, K., Fukunaga, R., Bagni, C., Proud, C. G., & Bramham, C. R. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.016 · Cited by 143
ERK2 enters the nucleus by a carrier-independent mechanism
Whitehurst, A. W., Wilsbacher, J. L., You, Y., Luby‐Phelps, K., Moore, M. S., & Cobb, M. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112495999 · Cited by 139
Phosphorylation of BRAF by AMPK Impairs BRAF-KSR1 Association and Cell Proliferation
Shen, C., Yuan, P., Pérez‐Lorenzo, R., Zhang, Y., Lee, S. X., Ou, Y., Asara, J. M., Cantley, L. C., & Zheng, B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.044 · Cited by 138
Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation
Mylona, A., Theillet, F., Foster, C., Cheng, T. M. K., Miralles, F., Bates, P. A., Selenko, P., & Treisman, R. (2016) · Science · doi:10.1126/science.aad1872 · Cited by 138
MED23 Mutation Links Intellectual Disability to Dysregulation of Immediate Early Gene Expression
Hashimoto, S., Boissel, S., Zarhrate, M., Rio, M., Münnich, A., Egly, J., & Colleaux, L. (2011) · Science · doi:10.1126/science.1206638 · Cited by 134
Karlsson, M. E., Mathers, J. E., Dickinson, R. J., Mandl, M., & Keyse, S. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406720200 · Cited by 132
Vemurafenib resistance reprograms melanoma cells towards glutamine dependence
Hernandez-Davies, J. E., Tran, T. Q., Reid, M. A., Rosales, K. R., Lowman, X. H., Pan, M., Moriceau, G., Yang, Y., Wu, J., Lo, R. S., et al. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0581-2 · Cited by 131
Coles, L. C., & Shaw, P. E. (2002) · Oncogene · doi:10.1038/sj.onc.1205302 · Cited by 126
Klf2 Is an Essential Factor that Sustains Ground State Pluripotency
Yeo, J.-C., Jiang, J., Tan, Z.-Y., Yim, D., Ng, J.-H., Göke, J., Kraus, P., Liang, H., Gonzales, K. A. U., Chong, H.-C., et al. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.04.015 · Cited by 124
The mitogen‐activated protein (MAP) kinase ERK induces tRNA synthesis by phosphorylating TFIIIB
Felton-Edkins, Z. A., Fairley, J. A., Graham, E. L., Johnston, I. M., White, R. J., & Scott, P. H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg240 · Cited by 121
Activity of the MAP kinase ERK2 is controlled by a flexible surface loop
Zhang, J., Zhang, F. P. Y., Ebert, D. J., Cobb, M. H., & Goldsmith, E. J. (1995) · Structure · doi:10.1016/s0969-2126(01)00160-5 · Cited by 121
Molecular basis for G‐actin binding to RPEL motifs from the serum response factor coactivator MAL
Mouilleron, S., Guettler, S., Langer, C. A., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.235 · Cited by 115
Bergeron, J. J. M., Guglielmo, G. M. D., Dahan, S., Dominguez, M., & Posner, B. I. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014659 · Cited by 110
Gallic, L. L., Sgouras, D. N., Beal, G., & Mavrothalassitis, G. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4121 · Cited by 106
Göke, J., Chan, Y.-S., Yan, J., Vingron, M., & Ng, H. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.030 · Cited by 105
Muehlich, S., Wang, R., Lee, S.-M., Lewis, T. C., Dai, C., & Prywes, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00427-08 · Cited by 104
Squires, M. S., NIXON, P. M., & Cook, S. J. (2002) · Biochemical Journal · doi:10.1042/bj20020372 · Cited by 103
van Berlo, J. H., Elrod, J. W., Aronow, B. J., Pu, W. T., & Molkentin, J. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104499108 · Cited by 101
Yang, R., Li, X., Wu, Y., Zhang, G., Liu, X., Li, Y., Bao, Y., Yang, W., & Cui, H. (2020) · Oncogene · doi:10.1038/s41388-020-1199-2 · Cited by 101
Erk signaling is indispensable for genomic stability and self-renewal of mouse embryonic stem cells
Chen, H., Guo, R., Zhang, Q., Guo, H., Yang, M., Wu, Z., Gao, S., Liu, L., & Chen, L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516319112 · Cited by 100
Zwang, Y., Sas‐Chen, A., Drier, Y., Shay, T., Avraham, R., Lauriola, M., Shema, E., Nili, E. L., Jacob‐Hirsch, J., Amariglio, N., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.017 · Cited by 100
Voisin, L., Saba-El-Leil, M. K., Julien, C., Frémin, C., & Meloche, S. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00131-10 · Cited by 100
ERK and RhoA Differentially Regulate Pseudopodia Growth and Retraction during Chemotaxis
Brahmbhatt, A. A., & Klemke, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211873200 · Cited by 98
Poortinga, G., Wall, M., Sanij, E., Siwicki, K., Ellul, J., Brown, D. V., Holloway, T. P., Hannan, R. D., & McArthur, G. A. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1205 · Cited by 98
Iritani, B. M., Delrow, J. J., Grandori, C., Gomez, I. G., Klacking, M., Carlos, L. S., & Eisenman, R. N. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf492 · Cited by 97
Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK
Mace, P. D., Wallez, Y., Egger, M. F., Dobaczewska, M. K., Robinson, H., Pasquale, E. B., & Riedl, S. J. (2013) · Nature Communications · doi:10.1038/ncomms2687 · Cited by 97
ERK reinforces actin polymerization to power persistent edge protrusion during motility
Mendoza, M. C., Vilela, M., Juarez, J. E., Blenis, J., & Danuser, G. M. (2015) · Science Signaling · doi:10.1126/scisignal.aaa8859 · Cited by 96
Nakamura, T., Gulick, J. M., Pratt, R., & Robbins, J. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903302106 · Cited by 94
Nuclear import of activated D-ERK by DIM-7, an importin family member encoded by the gene moleskin
Lorenzen, J. A., Baker, S., Denhez, F., Melnick, M. B., Brower, D. L., & Perkins, L. A. (2001) · Development · doi:10.1242/dev.128.8.1403 · Cited by 92
B-RAF Regulation of Rnd3 Participates in Actin Cytoskeletal and Focal Adhesion Organization
Klein, R. M., Spofford, L. S., Abel, E. V., Ortiz, A. E., & Aplin, A. E. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0895 · Cited by 92
ERF mutations reveal a balance of ETS factors controlling prostate oncogenesis
The International SU2C/PCF Prostate Cancer Dream Team, Bose, R., Karthaus, W. R., Armenia, J., Abida, W. M., Iaquinta, P. J., Zhang, Z., Wongvipat, J., Wasmuth, E. V., Shah, N., et al. (2017) · Nature · doi:10.1038/nature22820 · Cited by 90
Interplay of cell–cell contacts and RhoA/MRTF‐A signaling regulates cardiomyocyte identity
Dorn, T., Kornherr, J., Parrotta, E. I., Zawada, D. M., Ayetey, H., Santamaria, G., Iop, L., Mastantuono, E., Sinnecker, D., Goedel, A., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798133 · Cited by 90
Ruppert, C., Deiss, K., Herrmann, S., Vidal, M., Oezkur, M., Gorski, A., Weidemann, F., Lohse, M. J., & Lorenz, K. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221999110 · Cited by 86
Galan, J. A., Geraghty, K. M., Lavoie, G., Kanshin, E., Tcherkezian, J., Calabrese, V., Jeschke, G. R., Turk, B. E., Ballif, B. A., Blenis, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405601111 · Cited by 85
ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA
Fujishiro, S., Tanimura, S., Mure, S., Kashimoto, Y., Watanabe, K., & Kohno, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.066 · Cited by 84
Hwang, C. Y., Lee, C., & Kwon, K. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01758-08 · Cited by 82
MAPK and PI3K signaling: At the crossroads of neural crest development
Dinsmore, C. J., & Soriano, P. M. (2018) · Developmental Biology · doi:10.1016/j.ydbio.2018.02.003 · Cited by 82
Aguilar-Valles, A., Haji, N., De Gregorio, D., Matta-Camacho, E., Eslamizade, M. J., Popic, J., Sharma, V., Cao, R., Rummel, C., Tanti, A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04883-5 · Cited by 82
Ewing‐like sarcoma: An emerging family of round cell sarcomas
Renzi, S., Anderson, N. D., Light, N. D., & Gupta, A. A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27558 · Cited by 82
Dynamic lineage priming is driven via direct enhancer regulation by ERK
Hamilton, W. B., Mosesson, Y., Monteiro, R. S., Emdal, K. B., Knudsen, T. E., Francavilla, C., Barkai, N., Olsen, J. V., & Brickman, J. M. (2019) · Nature · doi:10.1038/s41586-019-1732-z · Cited by 80
Nakamura, T., Gulick, J. M., Colbert, M. C., & Robbins, J. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902230106 · Cited by 79
Villanueva, J., Yung, Y., Walker, J. L., & Assoian, R. K. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-10-0908 · Cited by 79
Panayiotou, R., Miralles, F., Pawlowski, R., Diring, J., Flynn, H. R., Skehel, M., & Treisman, R. (2016) · eLife · doi:10.7554/elife.15460 · Cited by 79
ERF Nuclear Shuttling, a Continuous Monitor of Erk Activity That Links It to Cell Cycle Progression
Gallic, L. L., Virgilio, L., Cohen, P., Biteau, B., & Mavrothalassitis, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1206-1218.2004 · Cited by 74
Subramanian, M., & Shaha, C. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.4.2330 · Cited by 70
Ogata, T., Naito, D., Nakanishi, N., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315359111 · Cited by 68
Choi, C., & Helfman, D. M. (2013) · Oncogene · doi:10.1038/onc.2013.341 · Cited by 67
Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity
Danson, C. M., Pocha, S. M., Bloomberg, G. B., & Cory, G. O. (2007) · Journal of Cell Science · doi:10.1242/jcs.013714 · Cited by 66
Bacterial Chemotaxis: Biochemistry of Behavior in a Single Cell
Ordal, G. (1985) · CRC Critical Reviews in Microbiology · doi:10.3109/10408418509104426 · Cited by 65
Redundancy in the World of MAP Kinases: All for One
Saba-El-Leil, M. K., Frémin, C., & Meloche, S. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00067 · Cited by 65
RSK Regulates PFK-2 Activity to Promote Metabolic Rewiring in Melanoma
Houlès, T., Gravel, S., Lavoie, G., Shin, S., Savall, M., Méant, A., Grondin, B., Gaboury, L. A., Yoon, S.-O., St‐Pierre, J., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2215 · Cited by 65
Sundberg-Smith, L. J., Doherty, J. T., Mack, C. P., & Taylor, J. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406013200 · Cited by 64
Lopez, J., Hesling, C., Prudent, J., Popgeorgiev, N., Gadet, R., Mikaélian, I., Rimokh, R., Gillet, G., & Gonzalo, P. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.21 · Cited by 60
Phosphorylation of WAVE Downstream of Mitogen-activated Protein Kinase Signaling
Miki, H., Fukuda, M., Nishida, E., & Takenawa, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27605 · Cited by 60
KLF4 Nuclear Export Requires ERK Activation and Initiates Exit from Naive Pluripotency
Dhaliwal, N. K., Miri, K., Davidson, S., Jarkass, H. T. E., & Mitchell, J. A. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.02.007 · Cited by 58
Bouveret, R., Waardenberg, A. J., Schonrock, N., Ramialison, M., Doan, T., de Jong, D., Bondue, A., Kaur, G., Mohamed, S., Fonoudi, H., et al. (2015) · eLife · doi:10.7554/elife.06942 · Cited by 57
Esnault, C., Gualdrini, F., Horswell, S. D., Kelly, G. P., Stewart, A., East, P., Matthews, N., & Treisman, R. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.005 · Cited by 55
Outstanding questions in developmental ERK signaling
Patel, A. L., & Shvartsman, S. Y. (2018) · Development · doi:10.1242/dev.143818 · Cited by 55
NANOG Is Multiply Phosphorylated and Directly Modified by ERK2 and CDK1 In Vitro
Brumbaugh, J., Russell, J. D., Yu, P., Westphall, M. S., Coon, J. J., & Thomson, J. A. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2013.12.005 · Cited by 54
Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex
Peleg, O., & Lim, R. Y. H. (2010) · Biological Chemistry · doi:10.1515/bc.2010.092 · Cited by 52
Verger, A., Buisine, E., Carrère‐Kremer, S., Wintjens, R. T., Flourens, A., Coll, J., Stéhelin, D., & Duterque‐Coquillaud, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010208200 · Cited by 50
Vasudevan, H. N., & Soriano, P. M. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.10.005 · Cited by 49
MEK1/2 Inhibition Decreases Lactate in BRAF-Driven Human Cancer Cells
Miniotis, M. F., Arunan, V., Eykyn, T. R., Marais, R., Workman, P., Leach, M. O., & Beloueche‐Babari, M. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-1969 · Cited by 49
Serine 111 Phosphorylation Regulates OCT4A Protein Subcellular Distribution and Degradation
Spelat, R., Ferro, F., & Curcio, F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.386755 · Cited by 46
Ueda, K., Yaoita, M., Niihori, T., Aoki, Y., & Okamoto, N. (2017) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.38337 · Cited by 46
RSK2 drives cell motility by serine phosphorylation of LARG and activation of Rho GTPases
Shi, G., Yang, W. S., Jin, L., Matter, M. L., & Ramos, J. W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708584115 · Cited by 46
Padul, V. G., Epari, S., Moiyadi, A. V., Shetty, P. M., & Shirsat, N. V. (2015) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22283 · Cited by 44
Aggregation of oral streptococci with Fusobacterium and Actinomyces.
KELSTRUP, J., & Td, F.-N. (1974) · PubMed · Cited by 44
The Nuclear Localization of ERK2 Occurs by Mechanisms Both Independent of and Dependent on Energy
Ranganathan, A., Yazicioglu, M. N., & Cobb, M. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513866200 · Cited by 43
Pullikuth, A., & Catling, A. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01178-09 · Cited by 41
Solution NMR Insights into Docking Interactions Involving Inactive ERK2
Piserchio, A., Warthaka, M., Devkota, A. K., Kaoud, T. S., Lee, S., Abramczyk, O., Ren, P., Dalby, K. N., & Ghose, R. (2011) · Biochemistry · doi:10.1021/bi2000559 · Cited by 41
Deletion of MAP2K2/MEK2: a novel mechanism for a RASopathy?
Nowaczyk, M. G. J. M., Thompson, B. A., Zeesman, S., Moog, U., Sanchez-Lara, P. A., Magoulas, P. L., Falk, R. E., Hoover-Fong, J. E., Batista, D., Amudhavalli, S. M., et al. (2013) · Clinical Genetics · doi:10.1111/cge.12116 · Cited by 41
Tan, Q., Brunetti, L., Rousseaux, M. W. C., Lu, H., Wan, Y., Revelli, J., Liu, Z., Goodell, M. A., & Zoghbi, H. Y. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716452115 · Cited by 41
The core and conserved role of MAL is homeostatic regulation of actin levelsPreprint
Salvany, L., Müller, J., Guccione, E., & Rørth, P. (2014) · Genes & Development · doi:10.1101/gad.237743.114 · Cited by 39
Optogenetics - Bringing light into the darkness of mammalian signal transduction
Mühlhäuser, W. W. D., Fischer, A., Weber, W., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.11.009 · Cited by 39
Lauriol, J., Cabrera, J. R., Roy, A., Keith, K., Hough, S. M., Damilano, F., Wang, B., Segarra, G. C., Flessa, M. E., Miller, L. E., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci80396 · Cited by 38
Vasjari, L., Bresan, S., Biskup, C. U., Pai, G. M., & Rubio, I. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1560205 · Cited by 38
Pharmacokinetic disposition of dimethyl sulfoxide administered intravenously to horses
Blythe, L. L., Craig, A. M., Christensen, J. M., et al. (1986) · American Journal of Veterinary Research · doi:10.2460/ajvr.1986.47.08.1739 · Cited by 36
Theodosakis, N., Held, M. A., Marzuka-Alcalá, A., Meeth, K. M., Micevic, G., Long, G. V., Scolyer, R. A., Stern, D. F., & Bosenberg, M. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0080 · Cited by 36
Regulatory roles of conserved phosphorylation sites in the activation T-loop of the MAP kinase ERK1
Lai, S., & Pelech, S. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-07-0527 · Cited by 36
Negative feedback via RSK modulates Erk‐dependent progression from naïve pluripotency
Nett, I., Mulas, C., Gatto, L., Lilley, K. S., & Smith, A. G. (2018) · EMBO Reports · doi:10.15252/embr.201745642 · Cited by 36
ERK signaling promotes cell motility by inducing the localization of myosin 1E to lamellipodial tips
Tanimura, S., Hashizume, J., Arichika, N., Watanabe, K., Ohyama, K., Takeda, K., & Kohno, M. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201503123 · Cited by 35
Single-Cell Imaging of ERK Signaling Using Fluorescent Biosensors
Pargett, M., Gillies, T. E., Teragawa, C., Sparta, B., & Albeck, J. G. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7154-1_3 · Cited by 35
Sriskanthadevan-Pirahas, S., Deshpande, R., Lee, B., & Grewal, S. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007202 · Cited by 35
ERK Signals: Scaffolding Scaffolds?
Casar, B., & Crespo, P. (2016) · Front. Cell Dev. Biol. · doi:10.3389/fcell.2016.00049 · Cited by 34
Samson, S. C., Elliott, A., Mueller, B., Kim, Y., Carney, K. R., Bergman, J. P., Blenis, J., & Mendoza, M. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007431 · Cited by 32
ERK2 phosphorylation of serine 77 regulates Bmf pro-apoptotic activity
Shao, Y., & Aplin, A. E. (2012) · Cell Death and Disease · doi:10.1038/cddis.2011.137 · Cited by 31
Time-resolved Phosphoproteome Analysis of Paradoxical RAF Activation Reveals Novel Targets of ERK
Kubiniok, P., Lavoie, H., Therrien, M., & Thibault, P. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.065128 · Cited by 31
Self-citationWoodrow, M. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00122-8 · Cited by 30
Piserchio, A., Warthaka, M., Kaoud, T. S., Callaway, K., Dalby, K. N., & Ghose, R. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702973114 · Cited by 26
Yin, J. C., Platt, M. J., Tian, X., Wu, X., Backx, P. H., Simpson, J. A., Araki, T., & Neel, B. G. (2017) · Nature Communications · doi:10.1038/ncomms15518 · Cited by 26
The EGF/Ras pathway controls growth in Drosophila via ribosomal RNA synthesis
Sriskanthadevan-Pirahas, S., Lee, J., & Grewal, S. (2018) · Developmental Biology · doi:10.1016/j.ydbio.2018.04.006 · Cited by 24
ERF deletion rescues RAS deficiency in mouse embryonic stem cellsPreprint
Mayor‐Ruiz, C., Olbrich, T., Drosten, M., Lecona, E., Vega-Sendino, M., Ortega, S., Domı́nguez, O., Barbacid, M., Ruiz, S., & Fernández-Capetillo, Ó. (2018) · Genes & Development · doi:10.1101/gad.310086.117 · Cited by 17
Strategies for Engineering and Rewiring Kinase Regulation
McCormick, J. W., Pincus, D., Resnekov, O., & Reynolds, K. A. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.11.005 · Cited by 17
Boucher, M.-J., Morisset, J., Vachon, P. H., Reed, J. C., Lain�, J., & Rivard, N. (2000) · Journal of Cellular Biochemistry · doi:10.1002/1097-4644(20001201)79:3
Flagged first, then by citations
Cited by
Sorted by citations
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
RAF-MEK-ERK pathway in cancer evolution and treatment
Ullah, R., Yin, Q., Snell, A. H., & Wan, L. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.05.010 · Cited by 553
MAPK/ERK Signaling Pathway in Hepatocellular Carcinoma
Moon, H., & Ro, S. W. (2021) · Cancers · doi:10.3390/cancers13123026 · Cited by 326
Endocytosis in the context-dependent regulation of individual and collective cell properties
Sigismund, S., Lanzetti, L., Scita, G., & Di Fiore, P. P. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00375-5 · Cited by 132
Determining the ERK-regulated phosphoproteome driving KRAS-mutant cancer
Klomp, J. E., Diehl, J. N., Klomp, J. A., Edwards, A. C., Yang, R., Morales, A. J., Taylor, K. E., Drizyte-Miller, K., Bryant, K. L., Schaefer, A., et al. (2024) · Science · doi:10.1126/science.adk0850 · Cited by 83
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
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