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A conserved docking motif in MAP kinases common to substrates, activators and regulators
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.
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“The majority of MAPK regulatory proteins investigated thus far contain KIMs.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [21]
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Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
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-citationBmi-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
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Items 401–500 of 821
Pullikuth, A., & Catling, A. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01178-09 · Cited by 41
Beck, M., Schirmacher, P., & Singer, S. (2017) · Journal of Hepatology · doi:10.1016/j.jhep.2017.06.021 · Cited by 37
Sours, K. M., Kwok, S. C., Rachidi, T., Lee, T., Ring, A. Y., Hoofnagle, A. N., Resing, K. A., & Ahn, N. G. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.04.044 · Cited by 38
Ang, B. K., Lim, C. Y., Koh, S. S., Sivakumar, N., Taib, S., Lim, K. B., Ahmed, S., Rajagopal, G., & Ong, S. H. (2007) · Journal of Molecular Signaling · doi:10.1186/1750-2187-2-1 · Cited by 38
Moustafa, K., Vos, D. D., Leprince, A., Savouré, A., & Laurière, C. (2008) · Scholarly Research Exchange · doi:10.3814/2008/143656 · Cited by 38
Lee, S., Ayrapetov, M. K., Kemble, D. J., Parang, K., & Sun, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508120200 · Cited by 38
Radial Spoke Protein 3 Is a Mammalian Protein Kinase A-anchoring Protein That Binds ERK1/2
Jivan, A., Earnest, S. A., Juang, Y.-C. A., & Cobb, M. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.048181 · Cited by 38
Aoyama, K., Nagata, M., Oshima, K., Matsuda, T., & Aoki, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100408200 · Cited by 38
RetractedHow do pleiotropic kinase hubs mediate specific signaling by TNFR superfamily members?
Schröfelbauer, B., & Hoffmann, A. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01060.x · Cited by 37
Πολυχρονόπουλος, Σ., Verykokakis, M., Yazicioglu, M. N., Sakarellos‐Daitsiotis, M., Cobb, M. H., & Mavrothalassitis, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605185200 · Cited by 37
Martin, M. C., Allan, L. A., Mancini, E. J., & Clarke, P. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705647200 · Cited by 37
Remote hot spots mediate protein substrate recognition for the Cdc25 phosphatase
Sohn, J., Kristjánsdóttir, K., Safi, A., Parker, B., Kiburz, B. M., & Rudolph, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407663101 · Cited by 37
Philipova, R., & Whitaker, M. (2005) · Journal of Cell Science · doi:10.1242/jcs.02683 · Cited by 37
Pouysségur, J. (2000) · Science · doi:10.1126/science.290.5496.1515 · Cited by 37
Asp, E., & Sunnerhagen, P. (2003) · Molecular Genetics and Genomics · doi:10.1007/s00438-002-0786-y · Cited by 37
Glatz, G., Gógl, G., Alexa, A., & Reményi, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.452235 · Cited by 40
Won, A. P., Garbarino, J. E., & Lim, W. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016337108 · Cited by 36
Dynamic single cell measurements of kinase activity by synthetic kinase activity relocation sensors
Durandau, E., Aymoz, D., & Pelet, S. B. (2015) · BMC Biology · doi:10.1186/s12915-015-0163-z · Cited by 36
Dada, L. A., Bittar, H. E. T., Welch, L. C., Vagin, O., Deiss‐Yehiely, N., Kelly, A. M., Baker, M. R., Capri, J. R., Cohn, W., Whitelegge, J. P., et al. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00813-15 · Cited by 35
Sammons, R. M., Perry, N. A., Li, Y., Cho, E. J., Piserchio, A., Zamora‐Olivares, D., Ghose, R., Kaoud, T. S., Debevec, G., Bartholomeusz, C., et al. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00093 · Cited by 36
Zheng, Z., Li, M., Jiang, P., Sun, N., & Lin, S. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.174885 · Cited by 37
Gibbs, P., Miralem, T., Lerner‐Marmarosh, N., Tudor, C., & Maines, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.279612 · Cited by 36
Docking interactions of the JNK scaffold protein WDR62
Cohen‐Katsenelson, K., Wasserman, T., Khateb, S., Whitmarsh, A. J., & Aronheim, A. (2011) · Biochemical Journal · doi:10.1042/bj20110284 · Cited by 37
Armstrong, S. P., Caunt, C. J., & McArdle, C. A. (2009) · Molecular Endocrinology · doi:10.1210/me.2008-0333 · Cited by 38
Molina, D. M., Grewal, S., & Bardwell, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510590200 · Cited by 37
Erk phosphorylates threonine 42 residue of ribosomal protein S3
Kim, H. D., Lee, J. Y., & Kim, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.079 · Cited by 36
Differential effects of stress stimuli on a JNK-inactivating phosphatase
Theodosiou, A. M., & Ashworth, A. (2002) · Oncogene · doi:10.1038/sj.onc.1205309 · Cited by 36
Targeting ERK beyond the boundaries of the kinase active site in melanoma
Sammons, R. M., Ghose, R., Tsai, K. Y., & Dalby, K. N. (2019) · Molecular Carcinogenesis · doi:10.1002/mc.23047 · Cited by 37
Finch, A. R., Caunt, C. J., Perrett, R. M., Tsaneva-Atanasova, K. T., & McArdle, C. A. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2011.12.021 · Cited by 37
Nagasaka, K., Seiki, T., Yamashita, A., Massimi, P., Subbaiah, V. K., Thomas, M., Kranjec, C., Kawana, K., Nakagawa, S., Yano, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053752 · Cited by 35
VRK3-mediated inactivation of ERK signaling in adult and embryonic rodent tissues
Kang, T., & Kim, K. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.011 · Cited by 35
Kliche, J., & Ivarsson, Y. (2022) · Biochemical Journal · doi:10.1042/bcj20200714 · Cited by 33
Jo, C., Cho, S., & Jo, S. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225128 · Cited by 34
Intramolecular Dephosphorylation of ERK by MKP3
Kim, Y., Rice, A. E., & Denu, J. M. (2003) · Biochemistry · doi:10.1021/bi035346b · Cited by 34
Sweeney, E. E., Burga, R. A., Li, C., Zhu, Y., & Fernandes, R. (2016) · Scientific Reports · doi:10.1038/srep37035 · Cited by 34
MKP-1 contributes to oxidative stress-induced apoptosis via inactivation of ERK1/2 in SH-SY5Y cells
Kim, G. S., Choi, Y. K., Song, S. S., Kim, W.-K., & Han, B. H. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.10.143 · Cited by 33
Determinants That Control the Specific Interactions between TAB1 and p38α
Zhou, H., Zheng, M., Chen, J., Xie, C., Kolatkar, A. R., Zarubin, T., Ye, Z., Akella, R., Lin, S., Goldsmith, E. J., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3824-3834.2006 · Cited by 34
Hamel, L., Benchabane, M., Nicole, M.-C., Major, I. T., Morency, M., Pelletier, G., Beaudoin, N., Sheen, J., & Séguin, A. (2011) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.178343 · Cited by 34
Kim, S.-H., Kwon, H., Kim, Y. S., Ryu, J.-H., Kim, K., Ahn, Y., Lee, W., & Choi, K. (2001) · Biochemical Journal · doi:10.1042/bj3610143 · Cited by 34
Ultrasensitization: Switch-Like Regulation of Cellular Signaling by Transcriptional Induction
Legewie, S., Blüthgen, N., Schäfer, R., & Herzel, H. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0010054 · Cited by 34
Phosphorylation of the mitochondrial protein Sab by stress-activated protein kinase 3
Court, N. W., Kuo, I. Y., Quigley, O., & Bogoyevitch, M. A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.04.148 · Cited by 34
Tárrega, C., Blanco-Aparicio, C., Muñoz, J. J., & Pulido, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108874200 · Cited by 33
Levin‐Salomon, V., Maayan, I., Avrahami‐Moyal, L., Marbach, I., Livnah, O., & Engelberg, D. (2008) · Biochemical Journal · doi:10.1042/bj20081335 · Cited by 33
Long-term dynamics of multisite phosphorylation
RUBINSTEIN, B. Y., Mattingly, H. H., Berezhkovskii, A. M., & Shvartsman, S. Y. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-03-0137 · Cited by 33
Regulation of atypical MAP kinases ERK3 and ERK4 by the phosphatase DUSP2
Perander, M., Al‐Mahdi, R., Jensen, T. C., Nunn, J. A. L., Kildalsen, H., Johansen, B., Gabrielsen, M., Keyse, S. M., & Seternes, O. M. (2017) · Scientific Reports · doi:10.1038/srep43471 · Cited by 36
Defnet, A. E., Huang, W., Polischak, S., Yadav, S. K., Kane, M. A., Shapiro, P., & Deshpande, D. A. (2019) · The FASEB Journal · doi:10.1096/fj.201900680r · Cited by 33
Wang, Z., Zhao, F., Tang, M.-Q., Chen, T., Bao, L.-L., Cao, J. W., Li, Y., Yang, Y., Zhu, K., Liu, S., et al. (2019) · Plant Science · doi:10.1016/j.plantsci.2019.110362 · Cited by 33
The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution
Akella, R., Min, X., Wu, Q., Gardner, K. H., & Goldsmith, E. J. (2010) · Structure · doi:10.1016/j.str.2010.09.015 · Cited by 31
The Molecular Mechanism of MAPK / ERK Inactivation
Yao, Z., & Seger, R. (2004) · Current Genomics · doi:10.2174/1389202043349309 · Cited by 32
ERK1/2/MAPK pathway-dependent regulation of the telomeric factor TRF2
Picco, V., Coste, I., Giraud-Panis, M.-J. E., Renno, T., Gilson, É., & Pagès, G. (2016) · Oncotarget · doi:10.18632/oncotarget.10316 · Cited by 32
MAPKAP kinase MK2 maintains self‐renewal capacity of haematopoietic stem cells
Schwermann, J., Rathinam, C., Schubert, M., Schumacher, S., Noyan, F., Koseki, H., Kotlyarov, A., Klein, C., & Gaestel, M. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.100 · Cited by 30
Development of Extracellular Signal-Regulated Kinase Inhibitors
Burkhard, K. A., Smith, S., Deshmukh, R. R., MacKerell, A. D., & Shapiro, P. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609789044416 · Cited by 31
Beaudry, K., Langlois, M., Montagne, A., Cagnol, S., Carrier, J. C., & Rivard, N. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27420 · Cited by 30
Katz, S., & Aronheim, A. (2002) · Biochemical Journal · doi:10.1042/bj20021127 · Cited by 31
Jung, K., Samadani, R., Chauhan, J., Nevels, K. J., Yap, J. L., Zhang, J., Worlikar, S. A., Lanning, M. E., Chen, L., Ensey, M., et al. (2013) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob40199e · Cited by 30
Beyond conventional biomass valorisation: pyrolysis-derived products for biomedical applications
Hamzah, M. A. A. M., Hasham, R., Malek, N. A. N. N., Hashim, Z., Yahayu, M., Razak, F. I. A., & Zakaria, Z. A. (2022) · Biofuel Research Journal · doi:10.18331/brj2022.9.3.2 · Cited by 30
Fernandes, N., Bailey, D. E., Vranken, D. L. V., & Allbritton, N. L. (2007) · ACS Chemical Biology · doi:10.1021/cb700158q · Cited by 29
Bassi, R., Burgoyne, J. R., Nicola, G. F. D., Rudyk, O., DeSantis, V., Charles, R. L., Eaton, P., & Marber, M. S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785410 · Cited by 30
Waetzig, G. H., & Schreiber, S. (2003) · Alimentary Pharmacology & Therapeutics · doi:10.1046/j.1365-2036.2003.01642.x · Cited by 31
Wolter, S., Mushinski, J. F., Saboori, A. M., Resch, K., & Kracht, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105800200 · Cited by 30
Wang, L., Zhong, Y., Li, Y., Yu, F., Brindley, P. J., McManus, D. P., Wei, D., Han, Z., Feng, Z., Li, Y., et al. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.055 · Cited by 29
Baker, S., Lorenzen, J. A., Miller, S. W., Bunch, T. A., Jannuzi, A. L., Ginsberg, M. H., Perkins, L. A., & Brower, D. L. (2002) · Genetics · doi:10.1093/genetics/162.1.285 · Cited by 29
Identification of mitogen-activated protein kinase homologues from Leishmania mexicana
Wiese, M., Wang, Q. A., & Görcke, I. (2003) · International Journal for Parasitology · doi:10.1016/s0020-7519(03)00252-2 · Cited by 29
MEK partner 1 (MP1): Regulation of oligomerization in MAP kinase signaling
Sharma, C., Vomastek, T., Tarcsafalvi, A., Catling, A. D., Schaeffer, H. J., Eblen, S. T., & Weber, M. J. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20344 · Cited by 29
A PARP1-ERK2 synergism is required for the induction of LTP
Visochek, L., Grigoryan, G., Kalal, A. A., Milshtein-Parush, H., Gazit, N., Slutsky, I., Yeheskel, A., Shainberg, A., Castiel, A., Seger, R., et al. (2016) · Scientific Reports · doi:10.1038/srep24950 · Cited by 28
Substrates of the MAPK Slt2: Shaping Yeast Cell Integrity
González-Rubio, G., Sastre-Vergara, L., Molina, M., Martı́n, H., & Fernández‐Acero, T. (2022) · Journal of Fungi · doi:10.3390/jof8040368 · Cited by 28
Wang, T., Liu, M., Wu, Y. B., Tian, Y., Han, Y., Liu, C., Hao, J., & Fan, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911129 · Cited by 28
Heat Shock Protein 27 Mediated Signaling in Viral Infection
Rajaiya, J., Yousuf, M. A., Singh, G., Stanish, H., & Chodosh, J. (2012) · Biochemistry · doi:10.1021/bi3007127 · Cited by 29
Importance of Domain Closure for the Autoactivation of ERK2
Barr, D. A., Oashi, T., Burkhard, K. A., Lucius, S., Samadani, R., Zhang, J., Shapiro, P., MacKerell, A. D., & van der Vaart, A. (2011) · Biochemistry · doi:10.1021/bi200503a · Cited by 28
Zhou, W., Feng, X., Wu, Y., Benge, J., Zhang, Z., & Chen, Z. (2009) · Cell Research · doi:10.1038/cr.2009.95 · Cited by 28
Wang, F., Wang, C., Yan, Y., Jia, H., & Guo, X. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00689 · Cited by 28
The Nuclear Translocation of ERK
Berti, D. A., & Seger, R. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6424-6_13 · Cited by 28
Singh, A. K., Nath, O., Singh, S., Kumar, S., & Singh, I. K. (2017) · Plant Gene · doi:10.1016/j.plgene.2017.12.001 · Cited by 28
Parker, B. W., Goncz, E., Krist, D. T., Statsyuk, A. V., Nesvizhskii, A. I., & Weiss, E. L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819533116 · Cited by 31
Perander, M., Åberg, E., Johansen, B., Dreyer, B., Guldvik, I. J., Outzen, H., Keyse, S. M., & Seternes, O. M. (2008) · Biochemical Journal · doi:10.1042/bj20071369 · Cited by 28
Callaway, K., Rainey, M. A., & Dalby, K. N. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.11.002 · Cited by 26
Neurocysticercosis: a review on status in India, management, and current therapeutic interventions
Ahmad, R., Khan, T., Ahmad, B., Misra, A., & Balapure, A. K. (2016) · Parasitology Research · doi:10.1007/s00436-016-5278-9 · Cited by 27
Yu, M., Wang, R., Xia, J.-Q., Li, C., Xu, Q.-H., Wang, Y., Wang, Y.-Y., & Zhang, D. (2023) · Plant Science · doi:10.1016/j.plantsci.2023.111621 · Cited by 27
Belozerov, V. E., Lin, Z., Gingras, A., McDermott, J. C., & Siu, K. W. M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00232-12 · Cited by 27
Chen, Y.-S., Huang, W.-H., Hong, S., Tsay, Y., & Chen, P. (2008) · Journal of Virology · doi:10.1128/jvi.00656-08 · Cited by 27
Hill, Z. B., Perera, B. G. K., Andrews, S., & Maly, D. J. (2011) · ACS Chemical Biology · doi:10.1021/cb200387g · Cited by 28
SUDO, T., Yagasaki, Y., Hama, H., Watanabe, N., & Osada, H. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6529 · Cited by 27
Zhan, X., Wishart, M. J., & Guan, K. (2001) · Chemical Reviews · doi:10.1021/cr000245u · Cited by 27
Nguyen, T., Ruan, Z., Oruganty, K., & Kannan, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119636 · Cited by 26
Nek2A specifies the centrosomal localization of Erk2
Lou, Y., Xie, W., Zhang, D., Yao, J.-H., Luo, Z.-F., Wang, Y., Shi, Y., & Yao, X. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.171 · Cited by 26
Pseudophosphatase MK‐STYX: the atypical member of the MAP kinase phosphatases
Hinton, S. D. (2020) · FEBS Journal · doi:10.1111/febs.15426 · Cited by 25
Substrate-Dependent Control of ERK Phosphorylation Can Lead to Oscillations
Liu, P., Kevrekidis, I. G., & Shvartsman, S. Y. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.025 · Cited by 29
Udomsinprasert, R., Bogoyevitch, M. A., & Ketterman, A. J. (2004) · Biochemical Journal · doi:10.1042/bj20040519 · Cited by 26
GIT1 is a novel MEK1–ERK1/2 scaffold that localizes to focal adhesions
Zhang, N., Cai, W., Yin, G., Nagel, D. J., & Berk, B. C. (2009) · Cell Biology International · doi:10.1042/cbi20090016 · Cited by 26
Specific Regulation of Cytokine-Dependent p38 MAP Kinase Activation by p62/SQSTM1
Kawai, K., Saito, A., SUDO, T., & Osada, H. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvn027 · Cited by 26
Sanz, V., Arozarena, I., & Crespo, P. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01598-2 · Cited by 26
Mitogen-activated protein kinase phosphatase-1 – a potential therapeutic target in metabolic disease
Flach, R. J. R., & Bennett, A. M. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.528395 · Cited by 25
Multiplexing the Quantitation of MAP Kinase Activities Using Differential Sensing
Zeng, L., Kaoud, T. S., Zamora‐Olivares, D., Bohanon, A. L., Li, Y., Pridgen, J. R., Ekpo, Y. E., Zhuang, D. L., Nye, J. R., Telles, M., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12757 · Cited by 25
Regulation of stress-activated MAP kinase pathways during cell fate decisions.
Takekawa, M., Kubota, Y., Nakamura, T., & Ichikawa, K. (2011) · PubMed Central · doi:10.18999/nagjms.73.1-2.1 · Cited by 25
Ultrasensitivity in Phosphorylation-Dephosphorylation Cycles with Little Substrate
Martins, B. M. C., & Swain, P. S. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003175 · Cited by 25
Molecular imaging of c-Met tyrosine kinase activity
Zhang, L., Virani, S., Zhang, Y., Bhojani, M. S., Burgess, T. L., Coxon, A., Galbán, C. J., Ross, B. D., & Rehemtulla, A. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.01.028 · Cited by 25
Peptides as Signaling Inhibitors for Mammalian MAP Kinase Cascades
Gaestel, M., & Kracht, M. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209788682299 · Cited by 27
Lee, C.-S., Dykema, K. J., Hawkins, D. M., Cherba, D., Webb, C. P., Furge, K. A., & Duesbery, N. S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017165 · Cited by 25
Salazar, C., & Höfer, T. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1378.093 · Cited by 25
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Metadata
- Authors
- Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E.
- Affiliations
- Kyoto University (JP)
- Corresponding author
- Nishida, Eisuke
- Venue
- Nature Cell Biology
- Published
- 2000-01-17
- Volume
- 2
- Issue
- 2
- Pages
- 110-116
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- 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
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