Cited by 821Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesMelanoma and MAPK Pathways

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

A conserved docking motif in MAP kinases common to substrates, activators and regulators

Tanoue, Takuji, Adachi, Makoto, Moriguchi, Tetsuo, Nishida, Eisuke·2000·Nature Cell Biology

Open this paper in CoChat — free account

Abstract

Mitogen-activated protein kinases (MAPKs) are specifically phosphorylated and activated by the MAPK kinases, phosphorylate various targets such as MAPK-activated protein kinases and transcription factors, and are inactivated by specific phosphatases. Recently, docking interactions via the non-catalytic regions of MAPKs have been suggested to be important in regulating these reactions. Here we identify docking sites in MAPKs and in MAPK-interacting enzymes. A docking domain in extracellular-signal-regulated kinase (ERK), a MAPK, serves as a common site for binding to the MAPK kinase MEK1, the MAPK-activated protein kinase MNK1 and the MAPK phosphatase MKP3. Two aspartic acids in this domain are essential for docking, one of which is mutated in the sevenmaker mutant of Drosophila ERK/Rolled. A corresponding domain in the MAPKs p38 and JNK/SAPK also serves as a common docking site for their MEKs, MAPK-activated protein kinases and MKPs. These docking interactions increase the efficiency of the enzymatic reactions. These findings reveal a hitherto unidentified docking motif in MAPKs that is used in common for recognition of their activators, substrates and regulators.

Integrity signals

Registry

Crossref · 10.1038/35000065

Cites

42 of 42 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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
How MAP Kinases Are Regulated
Cobb, M. H., & Goldsmith, E. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14843 · Cited by 1,718
Regulation of transcription by MAP kinase cascades
Treisman, R. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80067-6 · Cited by 1,296
The MAP kinase cascade is essential for diverse signal transduction pathways
Nishida, E., & Gotoh, Y. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90019-j · Cited by 1,087
Self-citation
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
Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor
Duesbery, N. S., Webb, C. P., Leppla, S. H., Gordon, V. M., Klimpel, K. R., Copeland, T. D., Ahn, N. G., Oskarsson, M. K., Fukasawa, K., Paull, K. D., et al. (1998) · Science · doi:10.1126/science.280.5364.734 · Cited by 1,007
Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
Waskiewicz, A. J., Flynn, A., Proud, C. G., & Cooper, J. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1909 · Cited by 951
MAPKs: new JNK expands the group
Davis, R. J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90132-5 · Cited by 944
Protein kinase cascades activated by stress and inflammatory cytokines
Kyriakis, J. M., & Avruch, J. (1996) · BioEssays · doi:10.1002/bies.950180708 · Cited by 709
Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation
Khokhlatchev, A. V., Canagarajah, B. J., Wilsbacher, J. L., Robinson, M. J., Atkinson, M. A., Goldsmith, E. J., & Cobb, M. H. (1998) · Cell · doi:10.1016/s0092-8674(00)81189-7 · Cited by 675

Flagged first, then by citations

Show all 42 references

Sorted by citations

Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118
Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation
Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,400
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
ERK and p38 MAPK-Activated Protein Kinases: a Family of Protein Kinases with Diverse Biological Functions
Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540
Mechanisms and functions of p38 MAPK signalling
Cuadrado, A., & Nebreda, Á. R. (2010) · Biochemical Journal · doi:10.1042/bj20100323 · Cited by 1,720
ERK1/2 MAP kinases: Structure, function, and regulation
Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,719
The JNK signal transduction pathway
Weston, C. R. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(01)00258-1 · Cited by 1,551
Mechanisms of specificity in protein phosphorylation
Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451
Mammalian MAPK Signal Transduction Pathways Activated by Stress and Inflammation: A 10-Year Update
Kyriakis, J. M., & Avruch, J. (2012) · Physiological Reviews · doi:10.1152/physrev.00028.2011 · Cited by 1,529
Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
Kölch, W. (2000) · Biochemical Journal · doi:10.1042/bj3510289 · Cited by 1,443
Differential regulation and properties of MAPKs
Raman, M., Chen, W., & Cobb, M. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210392 · Cited by 1,430
The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions
Yoon, S., & Seger, R. (2006) · Growth Factors · doi:10.1080/02699050500284218 · Cited by 1,331
Mitogen-activated protein kinase cascades in plants: a new nomenclature
MAPK Group, Ichimura, K., Shinozaki, K., Tena, G., Sheen, J., Henry, Y., Champion, A., Kreis, M. E., Zhang, S., Heribert Hirt, A., et al. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(02)02302-6 · Cited by 1,265
The MEK/ERK cascade: From signaling specificity to diverse functions
Shaul, Y. D., & Seger, R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.10.005 · Cited by 969
MAP Kinases
Chen, Z., Gibson, T. B., Robinson, F. L., Silvestro, L., Pearson, G. W., Xu, B.-E., Wright, A., Vanderbilt, C. A., & Cobb, M. H. (2001) · Chemical Reviews · doi:10.1021/cr000241p · Cited by 809
Protein–protein interactions define specificity in signal transductionPreprint
Pawson, T. J., & Nash, P. (2000) · Genes & Development · doi:10.1101/gad.14.9.1027 · Cited by 780
Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases
Owens, D. M., & Keyse, S. M. (2007) · Oncogene · doi:10.1038/sj.onc.1210412 · Cited by 777
Complexity, Cross Talk and Integration of Plant MAP Kinase Signalling
Jonak, C. (2002) · Current Opinion in Plant Biology · doi:10.1016/s1369-5266(02)00285-6 · Cited by 710
Mapk signal specificity: The right place at the right time
Murphy, L. O., & Blenis, J. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.03.009 · Cited by 707
MAPK phosphatases — regulating the immune response
Liu, Y., Shepherd, E. G., & Nelin, L. D. (2007) · Nature reviews. Immunology · doi:10.1038/nri2035 · Cited by 679
ERK1/2 MAP kinases in cell survival and apoptosis
Lu, Z., & Xu, S. (2006) · IUBMB Life · doi:10.1080/15216540600957438 · Cited by 675
Mitogen‐activated protein kinase cascades in plant signaling
Zhang, M., & Zhang, S. (2022) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13215 · Cited by 621
Uses for JNK: the Many and Varied Substrates of the c-Jun N-Terminal Kinases
Bogoyevitch, M. A., & Kobe, B. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00025-06 · Cited by 584
Dual‐specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling
Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535
The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions
Keshet, Y., & Seger, R. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-795-2_1 · Cited by 642
Short Linear Motifs: Ubiquitous and Functionally Diverse Protein Interaction Modules Directing Cell Regulation
Roey, K. V., Uyar, B., Weatheritt, R. J., Dinkel, H., Seiler, M., Budd, A., Gibson, T. J., & Davey, N. E. (2014) · Chemical Reviews · doi:10.1021/cr400585q · Cited by 513
The ERK Cascade: Distinct Functions within Various Subcellular Organelles
Wortzel, I., & Seger, R. (2011) · Genes & Cancer · doi:10.1177/1947601911407328 · Cited by 563
The c-jun kinase/stress-activated pathway: Regulation, function and role in human disease
Johnson, G. L., & Nakamura, K. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.12.009 · Cited by 512
Differential PROTAC substrate specificity dictated by orientation of recruited E3 ligase
Smith, B. E., Wang, S. L., Jaime-Figueroa, S., Harbin, A., Wang, J., Hamman, B. D., & Crews, C. M. (2019) · Nature Communications · doi:10.1038/s41467-018-08027-7 · Cited by 517
WNK1 Regulates Phosphorylation of Cation-Chloride-coupled Cotransporters via the STE20-related Kinases, SPAK and OSR1
Moriguchi, T., Urushiyama, S., Hisamoto, N., Iemura, S.-I., Uchida, S., Natsume, T., Matsumoto, K., & Shibuyà, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510042200 · Cited by 479
Self-citation
The regulation of extracellular signal-regulated kinase (ERK) in mammalian cells
Ramos, J. W. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.04.009 · Cited by 493
The ERK Cascade: A Prototype of MAPK Signaling
Rubinfeld, H., & Seger, R. (2005) · Molecular Biotechnology · doi:10.1385/mb:31:2:151 · Cited by 468
Domains, Motifs, and Scaffolds: The Role of Modular Interactions in the Evolution and Wiring of Cell Signaling Circuits
Bhattacharyya, R. P., Reményi, A., Yeh, B. J., & Lim, W. A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142710 · Cited by 458
Docking domains and substrate-specificity determination for MAP kinases
Sharrocks, A. D., Yang, S.-H., & Galanis, A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01627-3 · Cited by 442
Structure and regulation of MAPK phosphatases
Farooq, A., & Zhou, M. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2003.12.008 · Cited by 460
Essential Role of p38 Mitogen-activated Protein Kinase in Cathepsin K Gene Expression during Osteoclastogenesis through Association of NFATc1 and PU.1
Matsumoto, M., Kogawa, M., Wada, S., Takayanagi, H., Tsujimoto, M., Katayama, S., Hisatake, K., & Nogi, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408795200 · Cited by 436
The complexity of mitogen-activated protein kinases (MAPKs) made simple
Krishna, M., & Narang, H. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8170-7 · Cited by 439
Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling
Pouysségur, J., Volmat, V., & Lenormand, P. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01135-8 · Cited by 420
MAPKAP kinases — MKs — two's company, three's a crowd
Gaestel, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1834 · Cited by 413
MAPKAP Kinase-2 Is a Cell Cycle Checkpoint Kinase that Regulates the G2/M Transition and S Phase Progression in Response to UV Irradiation
Manke, I. A., Nguyen, A., Lim, D., Stewart, M. Q., Elia, A. E. H., & Yaffe, M. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.021 · Cited by 416
The p38 Pathway: From Biology to Cancer Therapy
Martínez-Limón, A., Joaquin, M., Caballero, M., Posas, F., & de Nadal, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061913 · Cited by 429
From JNK to Pay Dirt: Jun Kinases, their Biochemistry, Physiology and Clinical Importance
Karin, M., & Gallagher, E. D. (2005) · IUBMB Life · doi:10.1080/15216540500097111 · Cited by 414
Exome sequencing identifies recurrent mutations in NF1 and RASopathy genes in sun-exposed melanomas
Krauthammer, M. O., Kong, Y., Bacchiocchi, A., Evans, P., Pornputtapong, N., Wu, C., McCusker, J. P., Ma, S., Cheng, E., Straub, R., et al. (2015) · Nature Genetics · doi:10.1038/ng.3361 · Cited by 417
Dexamethasone Causes Sustained Expression of Mitogen-Activated Protein Kinase (MAPK) Phosphatase 1 and Phosphatase-Mediated Inhibition of MAPK p38
Lasa, M., Abraham, S., Boucheron, C., Saklatvala, J., & Clark, A. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.22.7802-7811.2002 · Cited by 386
Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
Vitale, G., Bernardi, L., Napolitani, G., Mock, M., & Montecucco, C. (2000) · Biochemical Journal · doi:10.1042/bj3520739 · Cited by 355
Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
BIONDI, R. M., & NEBREDA, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20021641 · Cited by 334
A Network of Immediate Early Gene Products Propagates Subtle Differences in Mitogen-Activated Protein Kinase Signal Amplitude and Duration
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
Illuminating the dark phosphoproteome
Needham, E. J., Parker, B. L., Burykin, T., James, D. E., & Humphrey, S. J. (2019) · Science Signaling · doi:10.1126/scisignal.aau8645 · Cited by 336
Diverse physiological functions for dual-specificity MAP kinase phosphatases
Dickinson, R. J., & Keyse, S. M. (2006) · Journal of Cell Science · doi:10.1242/jcs.03266 · Cited by 329
Molecular basis of MAP kinase regulation
Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302
Signaling by G-protein-coupled receptor (GPCR): Studies on the GnRH receptor
Naor, Z. (2008) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2008.07.001 · Cited by 333
The PHD Domain of MEKK1 Acts as an E3 Ubiquitin Ligase and Mediates Ubiquitination and Degradation of ERK1/2
Lu, Z., Xu, S., Joazeiro, C. A. P., Cobb, M. H., & Hunter, T. R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00519-1 · Cited by 323
MAP kinase phosphatases.
Theodosiou, A. M., & Ashworth, A. (2002) · Genome biology · doi:10.1186/gb-2002-3-7-reviews3009 · Cited by 321
The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
Biondi, R. M., Kieloch, A., Currie, R. A., Deak, M., & Alessi, D. R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4380 · Cited by 377
Molecular recognitions in the MAP kinase cascades
Tanoue, T., & Nishida, E. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00112-2 · Cited by 324
Self-citation
MAPK machinery in plants
Taj, G., Agarwal, P., Grant, M., & Kumar, A. (2010) · Plant Signaling & Behavior · doi:10.4161/psb.5.11.13020 · Cited by 314
Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3b
Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302
Extracellular Signal-regulated Kinase Phosphorylates Tumor Necrosis Factor α-converting Enzyme at Threonine 735: A Potential Role in Regulated Shedding
Dı́az-Rodrı́guez, E., Montero, J. C., Esparı́s-Ogando, A., Yuste, L., & Pandiella, A. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-11-0561 · Cited by 308
Role of mitogen-activated protein kinases in plant immunity
Pedley, K. F., & Martin, G. B. (2005) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2005.07.006 · Cited by 301
Mature-onset obesity and insulin resistance in mice deficient in the signaling adapter p62
Rodriguez, A., Durán, A., Selloum, M., Champy, M.-F., Diez-Guerra, F. J., Flores, J. M., Serrano, M., Auwerx, J., Diaz-Meco, M. T., & Moscat, J. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.011 · Cited by 290
ERK2 but Not ERK1 Induces Epithelial-to-Mesenchymal Transformation via DEF Motif-Dependent Signaling Events
Shin, S., Dimitri, C. A., Yoon, S.-O., Dowdle, W. E., & Blenis, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.020 · Cited by 299
Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions
Tanoue, T., Maeda, R., Adachi, M., & Nishida, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.466 · Cited by 285
Self-citation
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
MAP kinase pathways: The first twenty years
Avruch, J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.11.006 · Cited by 298
The Ste5 Scaffold Allosterically Modulates Signaling Output of the Yeast Mating Pathway
Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., & Lim, W. A. (2006) · Science · doi:10.1126/science.1120941 · Cited by 281
EGF-Induced ERK Activation Promotes CK2-Mediated Disassociation of α-Catenin from β-Catenin and Transactivation of β-Catenin
Ji, H., Wang, J., Nika, H., Hawke, D., Keezer, S., Ge, Q., Fang, B., Fang, X., Fang, D., Litchfield, D. W., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.034 · Cited by 270
Distinct Binding Determinants for ERK2/p38α and JNK MAP Kinases Mediate Catalytic Activation and Substrate Selectivity of MAP Kinase Phosphatase-1
Slack, D. N., Seternes, O. M., Gabrielsen, M., & Keyse, S. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010966200 · Cited by 269
Regulation of MAP kinases by MAP kinase phosphatases
Kondoh, K., & Nishida, E. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.12.002 · Cited by 268
Self-citation
GnRH signaling, the gonadotrope and endocrine control of fertility
Bliss, S. P., Navratil, A. M., Xie, J., & Roberson, M. S. (2010) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2010.04.002 · Cited by 259
Targeting the JNK MAPK cascade for inhibition: basic science and therapeutic potential
Bogoyevitch, M. A., Boehm, I., Oakley, A. J., Ketterman, A. J., & Barr, R. K. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.016 · Cited by 270
OsWRKY30 is activated by MAP kinases to confer drought tolerance in rice
Shen, H., Liu, C., Zhang, Y., Meng, X.-P., Zhou, X. E., Chu, C., & Wang, X. (2012) · Plant Molecular Biology · doi:10.1007/s11103-012-9941-y · Cited by 263
DUSPs, to MAP kinases and beyond
Huang, C.-Y., & Tan, T.-H. (2012) · Cell & Bioscience · doi:10.1186/2045-3701-2-24 · Cited by 260
Multisite protein phosphorylation – from molecular mechanisms to kinetic models
Salazar, C., & Höfer, T. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07027.x · Cited by 257
Phosphorylation meets nuclear import: a review
Nardozzi, J. D., Lott, K., & Cingolani, G. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-32 · Cited by 251
The Arabidopsis Mitogen-Activated Protein Kinase Kinase MKK3 Is Upstream of Group C Mitogen-Activated Protein Kinases and Participates in Pathogen Signaling
Dóczi, R., Brader, G., Pettkó‐Szandtner, A., Rajh, I., Armin Djamei, A., Andrea Pitzschke, A., Teige, M., & Heribert Hirt, A. (2007) · The Plant Cell · doi:10.1105/tpc.106.050039 · Cited by 248
The roles of MAPKs in disease
Lawrence, M. C., Jivan, A., Shao, C., Duan, L., Goad, D. L., Zaganjor, E., Osborne, J. K., McGlynn, K., Stippec, S., Earnest, S. A., et al. (2008) · Cell Research · doi:10.1038/cr.2008.37 · Cited by 240
Dealing with osmostress through MAP kinase activation
de Nadal, E., Alepuz, P. M., & Posas, F. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf158 · Cited by 233
The dual-specificity MAP kinase phosphatases: critical roles in development and cancer
Bermúdez, O. M., Pagès, G., & Gimond, C. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00347.2009 · Cited by 241
Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins11Edited by J. Thornton
Landgraf, R., Xénarios, I., & Eisenberg, D. S. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4540 · Cited by 231
Distinct Cellular Functions of MK2
Kotlyarov, A., Yannoni, Y. M., Fritz, S., Laaß, K., Telliez, J., Pitman, D., Lin, L., & Gaestel, M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4827-4835.2002 · Cited by 230
TRANSCRIPTIONAL AND POST-TRANSCRIPTIONAL CONTROL OF GENE EXPRESSION IN INFLAMMATION
Kracht, M., & Saklatvala, J. (2002) · Cytokine · doi:10.1006/cyto.2002.0895 · Cited by 229
Rac-PAK Signaling Stimulates Extracellular Signal-Regulated Kinase (ERK) Activation by Regulating Formation of MEK1-ERK Complexes
Eblen, S. T., Slack, J. K., Weber, M. J., & Catling, A. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.17.6023-6033.2002 · Cited by 229
Bidirectional signals transduced by DAPK–ERK interaction promote the apoptotic effect of DAPK
Chen, C.-H., Wang, W., Kuo, J., Tsai, H.-C., Lin, J., Chang, Z.-F., & Chen, R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600510 · Cited by 221
Mitogen-activated protein kinase pathways in redox signaling
Torrès, M. (2003) · Frontiers in bioscience · doi:10.2741/999 · Cited by 221
DCX, a new mediator of the JNK pathway
Gdalyahu, A., Ghosh, I., Levy, T., Sapir, T., Sapoznik, S., Fishler, Y., Azoulai, D., & Reiner, O. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600079 · Cited by 221
Extracellular-Regulated Kinases: Signaling From Ras to ERK Substrates to Control Biological Outcomes
Eblen, S. T. (2018) · Advances in cancer research · doi:10.1016/bs.acr.2018.02.004 · Cited by 217
Nuclear Signaling of Plant MAPKs
Bigeard, J., & Hirt, H. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00469 · Cited by 223
Mechanisms of MAPK signalling specificity
Bardwell, L. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340837 · Cited by 217
SakA MAP kinase is involved in stress signal transduction, sexual development and spore viability in Aspergillus nidulans
Kawasaki, L., Sánchez, O., Shiozaki, K., & Aguirre, J. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03087.x · Cited by 207
SIMKK, a Mitogen-Activated Protein Kinase (MAPK) Kinase, Is a Specific Activator of the Salt Stress-Induced MAPK, SIMK
Kiegerl, S., Cardinale, F., Siligan, C., Gross, A., Baudouin, E., Liwosz, A., Eklöf, S., Till, S., Bögre, L., Heribert Hirt, A., et al. (2000) · The Plant Cell · doi:10.1105/tpc.12.11.2247 · Cited by 211
Single and Combined Silencing of ERK1 and ERK2 Reveals Their Positive Contribution to Growth Signaling Depending on Their Expression Levels
LeFloch, R., Pouysségur, J., & Lenormand, P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00800-07 · Cited by 212
Specific Inactivation and Nuclear Anchoring of Extracellular Signal-Regulated Kinase 2 by the Inducible Dual-Specificity Protein Phosphatase DUSP5
Mandl, M., Slack, D. N., & Keyse, S. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1830-1845.2005 · Cited by 206
Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability
Chen, H., Chuang, H., & Tan, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112668 · Cited by 210
Regulation of Hippo pathway transcription factor TEAD by p38 MAPK-induced cytoplasmic translocation
Lin, K. C., Moroishi, T., Meng, Z., Jeong, H.-S., Plouffe, S. W., Sekido, Y., Han, J., Park, H. W., & Guan, K. (2017) · Nature Cell Biology · doi:10.1038/ncb3581 · Cited by 206
Specificity of signaling by STAT1 depends on SH2 and C‐terminal domains that regulate Ser727 phosphorylation, differentially affecting specific target gene expression
Kovarik, P., Mangold, M., Ramsauer, K., Heidari, H., Steinborn, R., Zotter, A., Levy, D. E., Müller, M., & Decker, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.91 · Cited by 200
The receptor for advanced glycation end‐products (RAGE) directly binds to ERK by a D‐domain‐like docking site
Ishihara, K., Tsutsumi, K., Kawane, S., Nakajima, M., & Kasaoka, T. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00846-9 · Cited by 201
A differentially regulated AP 2/ ERF transcription factor gene cluster acts downstream of a MAP kinase cascade to modulate terpenoid indole alkaloid biosynthesis in Catharanthus roseus
Paul, P., Singh, S. K., Patra, B., Sui, X., Pattanaik, S., & Yuan, L. (2016) · New Phytologist · doi:10.1111/nph.14252 · Cited by 200
An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors
Seidel, J. J., & Graves, B. J. (2002) · Genes & Development · doi:10.1101/gad.950902 · Cited by 182

Authors: Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E.
Affiliations: Kyoto University (JP)
Corresponding author: Nishida, Eisuke
ORCID: Adachi, Makoto
Moriguchi, Tetsuo
Nishida, Eisuke
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2000-01-17
Volume: 2
Issue: 2
Pages: 110-116
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/35000065
OpenAlex: W2083117403
Cited by: 816
References: 42
Citations by year: 2026: 13 · 2025: 16 · 2024: 15 · 2023: 25 · 2022: 26 · 2021: 17 · 2020: 16 · 2019: 24 · 2018: 20 · 2017: 25 · 2016: 23 · 2015: 27 · 2014: 19 · 2013: 28 · 2012: 32
FWCI: 19.91
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
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 › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Keywords: mitogen-activated protein kinase, extracellular signal-regulated kinase, MEK1, MKP-3, MAPK phosphatase, p38 MAPK, SAPK/JNK, MAPK kinase, aspartic acid residues, protein-protein interaction, kinase activation, substrate recognition
MeSH terms: Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Tyrosine Phosphatases, Conserved Sequence, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Mitogen-Activated Protein Kinase 1, Amino Acid Motifs, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, p38 Mitogen-Activated Protein Kinases, MAP Kinase Kinase 1, Dual Specificity Phosphatase 6

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

A conserved docking motif in MAP kinases common to substrates, activators and regulators

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks