Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents
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The protein tyrosine phosphatases (PTPs) PTP-SL, STEP and HePTP are mitogen-activated protein kinase (MAPK) substrates and regulators that bind to MAPKs through a kinase-interaction motif (KIM) located in their non-catalytic regulatory domains. We have found that the binding of these PTPs to the MAPKs extracellular-signal-regulated kinase 1 and 2 (ERK1/2), and p38α is differentially determined by the KIM-adjacent C-terminal regions of the PTPs, which have been termed kinase-specificity sequences, and is influenced by reducing agents. Under control conditions, PTP-SL bound preferentially to ERK1/2, whereas STEP and HePTP bound preferentially to p38α. Under reducing conditions, the association of p38α with STEP or HePTP was impaired, whereas the association with PTP-SL was unaffected. On the other hand, the association of ERK1/2 with HePTP was increased under reducing conditions, whereas the association with STEP or PTP-SL was unaffected. In intact cells, PTP-SL and STEP distinctively regulated the kinase activity and the nuclear translocation of ERK1/2 and p38α. Our results suggest that intracellular redox conditions could modulate the activity and subcellular location of ERK1/2 and p38α by controlling their association with their regulatory PTPs.
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While the KIM is required for binding, residues outside the KIM contribute to both binding and specificity.
“While the KIM is required for binding, 38,39 multiple reports have shown that residues outside the KIM contribute to both binding and specificity.40,41”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [40]
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Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,118 · see citing works
Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,369 · see citing works
Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to Human
Widmann, C., Gibson, S. B., Jarpe, M. B., & Johnson, G. L. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.1.143 · Cited by 2,707 · see citing works
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 · see citing works
Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers
Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600 · see citing works
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 · see citing works
Organization and regulation of mitogen-activated protein kinase signaling pathways
Garrington, T. P., & Johnson, G. L. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80028-3 · Cited by 1,275 · see citing works
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 1,060 · see citing works
A conserved docking motif in MAP kinases common to substrates, activators and regulators
Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E. (2000) · Nature Cell Biology · doi:10.1038/35000065 · Cited by 816 · see citing works
Protein phosphatases and the regulation of mitogen-activated protein kinase signalling
Keyse, S. M. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00075-7 · Cited by 808 · see citing works
Components of a New Human Protein Kinase Signal Transduction Pathway
Zhou, G., Bao, Z., & Dixon, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12665 · Cited by 642 · see citing works
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 · see citing works
Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439 · see citing works
New Insights into the Control of MAP Kinase Pathways
English, J. M., Pearson, G. W., Wilsbacher, J. L., Swantek, J. L., Karandikar, M. S., Xu, S., & Cobb, M. H. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4687 · Cited by 434 · see citing works
Primary Structure of BMK1: A New Mammalian MAP Kinase
Lee, J. D., Ulevitch, R. J., & Han, J. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2189 · Cited by 345 · see citing works
Pulido, R., Zúñiga, Á., & Ullrich, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7337 · Cited by 320 · see citing works
Self-citationTanoue, T., Maeda, R., Adachi, M., & Nishida, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.466 · Cited by 285 · see citing works
Slack, D. N., Seternes, O. M., Gabrielsen, M., & Keyse, S. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010966200 · Cited by 269 · see citing works
Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation
Pelkey, K. A., Askalan, R., Paul, S., Kalia, L. V., Nguyen, T.-H., Pitcher, G. M., Salter, M. W., & Lombroso, P. J. (2002) · Neuron · doi:10.1016/s0896-6273(02)00633-5 · Cited by 208 · see citing works
Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase
Saxena, M., Williams, S., Taskén, K., & Mustelin, T. (1999) · Nature Cell Biology · doi:10.1038/13024 · Cited by 203 · see citing works
Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum.
Lombroso, P. J., Murdoch, G., & Lerner, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7242 · Cited by 188 · see citing works
Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420
Nguyen, T.-H., Liu, J., & Lombroso, P. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111683200 · Cited by 185 · see citing works
Abe, M. K., Kuo, W.-L., Hershenson, M. B., & Rosner, M. R. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1301 · Cited by 155 · see citing works
Blanco‐Aparicio, C., Torres, J., & Pulido, R. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.6.1129 · Cited by 151 · see citing works
Self-citationPaul, S., Snyder, G. L., Yokakura, H., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-15-05630.2000 · Cited by 148 · see citing works
Saxena, M., Williams, S., Brockdorff, J. L., Gilman, J., & Mustelin, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.11693 · Cited by 135 · see citing works
Zúñiga, Á., Torres, J., Úbeda, J., & Pulido, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21900 · Cited by 131 · see citing works
Self-citationERK8, a New Member of the Mitogen-activated Protein Kinase Family
Abe, M. K., Saelzler, M. P., Espinosa, R., Kahle, K. T., Hershenson, M. B., Beau, M. M. L., & Rosner, M. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112483200 · Cited by 127 · see citing works
Lombroso, P., Naegele, J. R., Sharma, E., & Lerner, M. R. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-07-03064.1993 · Cited by 119 · see citing works
Multiple Regions of MAP Kinase Phosphatase 3 Are Involved in Its Recognition and Activation by ERK2
Zhou, B., Wu, L., Shen, K., Zhang, J., Lawrence, D. S., & Zhang, Z. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009753200 · Cited by 116 · see citing works
Xu, B.-E., Wilsbacher, J. L., Collisson, T., & Cobb, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34029 · Cited by 109 · see citing works
Cloning and expression of an inducible lymphoid‐specific, protein tyrosine phosphatase (HePTPase)
Zanke, B., Suzuki, H., Kishihara, K., Mizzen, L., Minden, M., Pawson, A., & Mak, T. W. (1992) · European Journal of Immunology · doi:10.1002/eji.1830220134 · Cited by 101 · see citing works
Modular Structure of a Docking Surface on MAPK Phosphatases
Tanoue, T., Yamamoto, T., & Nishida, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202096200 · Cited by 78 · see citing works
Specificity Determinants in MAPK Signaling to Transcription Factors
Baršytė-Lovejoy, D., Galanis, Α., & Sharrocks, A. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108145200 · Cited by 77 · see citing works
Saxena, M., Williams, S., Gilman, J., & Mustelin, T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15340 · Cited by 76 · see citing works
Bult, A., Zhao, F., Dirkx, R. A., Raghunathan, A., Solimena, M., & Lombroso, P. J. (1997) · PubMed · Cited by 71 · see citing works
Dang, A., Frost, J. A., & Cobb, M. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19909 · Cited by 69 · see citing works
Gronda, M., Arab, S., Iafrate, B., Suzuki, H., & Zanke, B. W. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.20.6851-6858.2001 · Cited by 67 · see citing works
Ogata, M., 澤田, 元., Fujino, Y., & Hamaoka, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2337 · Cited by 57 · see citing works
Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTP
Adachi, M., Sekiya, M., Isobe, M., Kumura, Y., Ogita, Z.-I., Hinoda, Y., Imai, K., & Yachi, A. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81592-x · Cited by 56 · see citing works
Hendriks, W., Schepens, J., Brugman, C., Zeeuwen, P., & Wieringa, B. (1995) · Biochemical Journal · doi:10.1042/bj3050499 · Cited by 52 · see citing works
The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP
Pettiford, S. M., & Herbst, R. (2000) · Oncogene · doi:10.1038/sj.onc.1203408 · Cited by 47 · see citing works
Phosphotyrosine-specific Phosphatase PTP-SL Regulates the ERK5 Signaling Pathway
Buschbeck, M., Eickhoff, J., Sommer, M. N., & Ullrich, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202149200 · Cited by 45 · see citing works
Calcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP)
Nguyen, T., Paul, S., Xu, Y., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.01995.x · Cited by 44 · see citing works
Oh‐hora, M., Ogata, M., Mori, Y., Adachi, M., Imai, K., Kosugi, A., & Hamaoka, T. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.3.1282 · Cited by 42 · see citing works
van den Maagdenberg, A. M. J. M., Bächner, D., Schepens, J. T. G., Peters, W., Fransen, J. A. M., Wieringa, B., & Hendriks, W. J. A. J. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00802.x · Cited by 39 · see citing works
Tárrega, C., Blanco-Aparicio, C., Muñoz, J. J., & Pulido, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108874200 · Cited by 33 · see citing works
Self-citationRaghunathan, A., Matthews, G. A., Lombroso, P. J., & Naegele, J. R. (1996) · Developmental Brain Research · doi:10.1016/0165-3806(95)00176-x · Cited by 30 · see citing works
Szedlacsek, S. E., Aricescu, A. R., Fulga, T. A., Renault, L., & Scheidig, A. J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4890 · Cited by 21 · see citing works
Induction of protein‐tyrosine phosphatase LC‐PTP by IL‐2 in human T cells
Adachi, M., Sekiya, M., Ishino, M., et al. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80114-2 · Cited by 20 · see citing works
Watanabe, Y., Shiozuka, K., Ikeda, T., Hoshi, N., Hiraki, H., Suzuki, T., Hashimoto, S., & Kawashima, H. (1998) · Molecular Brain Research · doi:10.1016/s0169-328x(98)00100-4 · Cited by 19 · see citing works
Flagged first, then by citations
2 of the 53 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
ERK1/2 MAP kinases: Structure, function, and regulation
Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,642 · see citing works
Molecular basis of MAP kinase regulation
Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302 · see citing works
“While the KIM is required for binding,(38,39) multiple reports have shown that residues outside the KIM contribute to both binding and specificity.(40,41)”
BackgroundTargeting NMDA receptors in stroke: new hope in neuroprotection
Wu, Q. J., & Tymianski, M. (2018) · Molecular Brain · doi:10.1186/s13041-018-0357-8 · Cited by 320 · see citing works
“It dephosphorylates and inactivates a number of important synaptic signaling proteins including two of the mitogen activated protein kinases (MAPK): the extracellular signalregulated kinase (ERK), and stress response protein kinase p38 [122, 123].”
BackgroundXu, J., Kurup, P., Zhang, Y., Goebel-Goody, S., Wu, P. H., Hawasli, A. H., Baum, M., Bibb, J., & Lombroso, P. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2212-09.2009 · Cited by 293 · see citing works
Metabotropic Glutamate Receptor-Mediated Long-Term Depression: Molecular Mechanisms
Gladding, C. M., Fitzjohn, S. M., & Molnár, E. (2009) · Pharmacological Reviews · doi:10.1124/pr.109.001735 · Cited by 233 · see citing works
“Although ERK1/2 stimulates STEP translation, STEP can also dephosphorylate and inactivate ERK1/2 in addition to p38 MAPK (Muñoz et al., 2003; Paul et al., 2003).”
BackgroundZhang, Y., Venkitaramani, D. V., Gladding, C. M., Zhang, Y., Kurup, P. K., Molnár, E., Collingridge, G. L., & Lombroso, P. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2666-08.2008 · Cited by 191 · see citing works
Goody, S. M. G., Baum, M. L., Paspalas, C. D., Fernandez, S. M., Carty, N., Kurup, P. K., & Lombroso, P. J. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003053 · Cited by 159 · see citing works
Functions of p38 MAP Kinases in the Central Nervous System
Asih, P. R., Prikas, E., Stefanoska, K., Tan, A. R. P., Ahel, H. I., & Ittner, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.570586 · Cited by 158 · see citing works
“As such, p38 MAP kinase has been suggested as drug target for AD treatment (Munoz and Ammit, 2010).”
BackgroundXu, J., Chatterjee, M., Baguley, T. D., Brouillette, J., Kurup, P. K., Ghosh, D., Kanyo, J. E., Zhang, Y., Seyb, K. I., Ononenyi, C., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001923 · Cited by 144 · see citing works
“mitogen-activated protein kinase (MAPK) family members ERK1/2 and p38 [11,12], the tyrosine kinases Fyn and Pyk2 [13,14], the glutamate receptor GluN2B subunit of NMDARs (formerly termed NR2B) [6,15,16], and the GluA2 subunit of AMPAR (formerly termed GluR2) [16–18].”
BackgroundProtein tyrosine phosphatase variants in human hereditary disorders and disease susceptibilities
Hendriks, W. J. A. J., & Pulido, R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.05.022 · Cited by 113 · see citing works
Self-citationGenetic manipulation of STEP reverses behavioral abnormalities in a fragile X syndrome mouse model
Goebel‐Goody, S. M., Wilson‐Wallis, E. D., Royston, S., Tagliatela, S. M., Naegele, J. R., & Lombroso, P. J. (2012) · Genes, Brain and Behavior · doi:10.1111/j.1601-183x.2012.00781.x · Cited by 108 · see citing works
“…of Fyn, Pyk2, ERK1/2 and p38 inactivates these enzymes, whereas dephosphorylation of surface NMDARs and AMPARs promotes their endocytosis (Nguyen et al. 2002; Pelkey et al. 2002; Munoz et al. 2003; Paul et al. 2003; Snyder et al. 2005; Zhang et al. 2008; Venkitaramani et al. 2011).”
BackgroundProtein Phosphatases and Alzheimer's Disease
Braithwaite, S. P., Stock, J. B., Lombroso, P. J., & Nairn, A. C. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00012-2 · Cited by 106 · see citing works
“An important feature of STEP is the presence of a kinase-interacting motif (KIM domain) that is essential for substrate binding.(187,195) Notably, phosphorylation by protein kinase A at a serine residue within the KIM acts to inhibit the interaction of STEP with substrates,(196) and phosphorylation of the KIM domain c…”
Fan, J., Gladding, C. M., Wang, L., Zhang, L. Y. J., Kaufman, A. M., Milnerwood, A. J., & Raymond, L. A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.019 · Cited by 94 · see citing works
Striatal-enriched Protein-tyrosine Phosphatase (STEP) Regulates Pyk2 Kinase Activity
Xu, J., Kurup, P. K., Bartos, J. A., Patriarchi, T., Hell, J. W., & Lombroso, P. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.368654 · Cited by 91 · see citing works
Zhang, Y., Mei, Z., Wu, J., & Wang, Z. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801703200 · Cited by 84 · see citing works
Erkens, M., Tanaka, K., Cheron, G. A., Márquez‐Ruiz, J., Prigogine, C., Schepens, J. T. G., Kasri, N. N., Augustine, G. J., & Hendriks, W. J. A. J. (2015) · Molecular Brain · doi:10.1186/s13041-014-0092-8 · Cited by 82 · see citing works
Structural basis of p38α regulation by hematopoietic tyrosine phosphatase
Francis, D. M., Różycki, B., Koveal, D., Hummer, G., Page, R., & Peti, W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.707 · Cited by 79 · see citing works
“, it has recently become clear that residues outside the KIM are necessary to confer specificit”
Delaforge, E., Kragelj, J., Tengo, L., Palencia, A., Milles, S., Bouvignies, G., Salvi, N., Blackledge, M. J., & Jensen, M. R. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b12407 · Cited by 80 · see citing works
Receptor type protein tyrosine phosphatases (RPTPs) – roles in signal transduction and human disease
Xu, Y., & Fisher, G. J. (2012) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-012-0171-5 · Cited by 75 · see citing works
“Accumulating evidence supports that tyrosinephosphorylated Erk1/2/5 are PTPRR substrates (Buschbeck et al. 2002; Munoz et al. 2003; Pulido et al. 1998; Zuniga et al. 1999).”
BackgroundSaavedra, A., Giralt, A., Rué, L., Xifró, X., Xu, J., Ortega, Z., Lucas, J. J., Lombroso, P. J., Alberch, J., & Pérez‐Navarro, E. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3446-10.2011 · Cited by 71 · see citing works
“, 2008), leading to their endocytosis, and the kinases ERK1/2 (extracellular signal-regulated kinase 1/2), p38, and Fyn, thereby controlling the duration of their signal (Pulido et al., 1998; Nguyen et al., 2002; Muñoz et al., 2003; Paul et al., 2003).”
BackgroundSacco, F., Tinti, M., Palma, A., Ferrari, E., Nardozza, A. P., van Huijsduijnen, R. H., Takahashi, T., Castagnoli, L., & Cesareni, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.002758 · Cited by 70 · see citing works
Sherwin, J. R. A., Sharkey, A. M., Mihalyi, A., Simsa, P., Catalano, R. D., & D'Hooghe, T. M. (2008) · Human Reproduction · doi:10.1093/humrep/den078 · Cited by 66 · see citing works
“PTPRR contains a 16-amino-acid, kinase-interaction motif that binds specifically to, and inhibits, extracellular-signal-regulated kinase 1/2, a member of the mitogen-activated protein kinase family (Munoz et al., 2003).”
BackgroundQuantitative Analysis of ERK2 Interactions with Substrate Proteins
Burkhard, K. A., Chen, F., & Shapiro, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177899 · Cited by 62 · see citing works
Eswaran, J., von Kries, J. P., Marsden, B. D., Longman, E., Debreczeni, J. E., Ugochukwu, E., Turnbull, A., Lee, W. H., Knapp, S., & Barr, A. (2006) · Biochemical Journal · doi:10.1042/bj20051931 · Cited by 65 · see citing works
Zhou, X., Ferraris, J. D., Cai, Q., Agarwal, A., & Burg, M. B. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00463.2004 · Cited by 64 · see citing works
“Phosphorylation of p38 by MEKK3 increases its activity (48) and dephosphorylation by protein tyrosine phosphatases (PTPs) can decrease it (34).”
BackgroundZhang, Y.-Y., Wu, J.-W., & Wang, Z.-X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203786 · Cited by 63 · see citing works
STEP 61 is a substrate of the E3 ligase parkin and is upregulated in Parkinson’s disease
Kurup, P. K., Xu, J., Videira, R. A., Ononenyi, C., Baltazar, G., Lombroso, P. J., & Nairn, A. C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417423112 · Cited by 62 · see citing works
Zhang, Y., Kurup, P. K., Xu, J., Anderson, G. M., Greengard, P., Nairn, A. C., & Lombroso, P. J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07450.x · Cited by 55 · see citing works
Liu, X., Zhang, C., Lu, C., Lin, S., Wu, J., & Wang, Z. (2016) · Nature Communications · doi:10.1038/ncomms10879 · Cited by 55 · see citing works
Stanoev, A., Mhamane, A., Schuermann, K. C., Grecco, H. E., Stallaert, W., Baumdick, M. E., Brüggemann, Y., Joshi, M. S., Roda‐Navarro, P., Fengler, S., et al. (2018) · Cell Systems · doi:10.1016/j.cels.2018.06.006 · Cited by 54 · see citing works
“The tyrosine phosphatase PTPN14-Pez inhibits metastasis by altering protein trafficking.”
BackgroundChen, J., Zhao, X., Yuan, Y., & Jing, J. (2020) · Cancer Cell International · doi:10.1186/s12935-020-01315-7 · Cited by 55 · see citing works
Dabrowska, J., Hazra, R., Guo, J., Li, C., DeWitt, S., Xu, J., Lombroso, P. J., & Rainnie, D. G. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2013.07.032 · Cited by 53 · see citing works
The Role of Striatal-Enriched Protein Tyrosine Phosphatase (STEP) in Cognition
Fitzpatrick, C. J., & Lombroso, P. (2011) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2011.00047 · Cited by 47 · see citing works
“NEUROANATOMY REVIEW ARTICLE published: 29 July 2011 doi: 10.3389/fnana.2011.00047 The role of striatal-enriched protein tyrosine phosphatase (STEP) in cognition”
BackgroundInfluentialMAPK-specific tyrosine phosphatases: new targets for drug discovery?
Barr, A., & Knapp, S. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.08.005 · Cited by 46 · see citing works
McAlees, J. W., & Sanders, V. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01466-08 · Cited by 45 · see citing works
“HePTP is a constitutively active protein tyrosine phosphatase (PTP) in the cytoplasm of lymphocytes that binds to and regulates tyrosine phosphorylation of p38 and ERK1/2 MAPKs through its kinase interaction motif (41), with a preference for p38 MAPK (23).”
BackgroundTan, E. Y., Richard, C. L., Zhang, H., et al. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00238.2005 · Cited by 42 · see citing works
“Our preliminary studies have excluded the involvement of SHP-2, which in any case is usually coupled to an increase in ERK activation (13, 69), as well as SHP-1 and PTP1B: sodium stibogluconate, at a concentration of 100 M (105 g/ml), which is sufficient to inhibit these three PTPs (54), produced no change in the decr…”
BackgroundLarge-Scale Identification of Disease Genes Involved in Acute Myeloid Leukemia
Erkeland, S. J., Valkhof, M. G., Heijmans‐Antonissen, C., et al. (2004) · Journal of Virology · doi:10.1128/jvi.78.4.1971-1980.2004 · Cited by 41 · see citing works
“Interestingly, recent data suggest that PTPN5/STEP shows a preferential affinity for p38 mitogen-activated protein kinase in a redox-sensitive manner, leaving the Erk kinases largely unaffected (40).”
BackgroundHaddad, J. J. (2004) · International Immunopharmacology · doi:10.1016/j.intimp.2004.06.006 · Cited by 40 · see citing works
Menigatti, M., Cattaneo, E., Sabates–Bellver, J., Ilinsky, V. V., Went, P., Buffoli, F., Márquez, V. E., Jiricny, J., & Marra, G. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-124 · Cited by 39 · see citing works
“PTPRR-mediated dephosphorylation of ERKs 1, 2, and 5 prevents their translocation to the nucleus [30-33].”
Boguslawski, G., McGlynn, P. W., Harvey, K. A., & Kovala, A. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308625200 · Cited by 37 · see citing works
Tonicity-Dependent Regulation of Osmoprotective Genes in Mammalian Cells
Ferraris, J. D., & Burg, M. B. (2006) · KARGER eBooks · doi:10.1159/000096320 · Cited by 37 · see citing works
Altered MAP kinase phosphorylation and impaired motor coordination in PTPRR deficient mice
Chirivi, R. G. S., Noordman, Y. E., der Zee, C. E. E. M. V., & Hendriks, W. J. A. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04398.x · Cited by 36 · see citing works
“…in ERK1/2 hyperphosphorylation The reported interaction of PTPRR isoforms with several MAPKs (Pulido et al. 1998; Ogata et al. 1999; Buschbeck et al. 2002; Munoz et al. 2003) prompted us to investigate MAPK activity in mouse brain lysates through the monitoring of MAPK biphosphorylation levels.”
BackgroundMolecular mechanism of ERK dephosphorylation by striatal‐enriched protein tyrosine phosphatase
Li, R., Xie, D., Dong, J., Li, H., Li, K., Su, J., Chen, L., Xu, Y., Wang, H., Gong, Z., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12463 · Cited by 35 · see citing works
“KIM is linked to the STEP catalytic domain by the kinase-specificity sequence (KIS), which is involved in differential recognition of MAP kinases and is affected by reducing reagents (Munoz et al. 2003).”
BackgroundResultInfluentialBaguley, T. D., Xu, H., Chatterjee, M., Nairn, A. C., Lombroso, P. J., & Ellman, J. A. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401037h · Cited by 35 · see citing works
Role of Striatal-Enriched Tyrosine Phosphatase in Neuronal Function
Kamceva, M., Benedict, J., Nairn, A. C., & Lombroso, P. J. (2016) · Neural Plasticity · doi:10.1155/2016/8136925 · Cited by 33 · see citing works
“Two members of the MAPK family of proteins are STEP substrates, the extracellular signal-regulated kinases 1 and 2 (ERK1/2) and p38 [36–39].”
BackgroundResting and Active States of the ERK2:HePTP Complex
Francis, D. M., Różycki, B., Tortajada, A., Hummer, G., Peti, W., & Page, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2075136 · Cited by 32 · see citing works
PTPRR Protein Tyrosine Phosphatase Isoforms and Locomotion of Vesicles and Mice
Hendriks, W. J. A. J., Dilaver, G., Noordman, Y. E., Kremer, B. P. H., & Fransen, J. A. M. (2009) · The Cerebellum · doi:10.1007/s12311-008-0088-y · Cited by 32 · see citing works
“Association specificity is also influenced by a small sequence that is located in between the KIM and the PTP domain [32].”
BackgroundThe Molecular Mechanism of MAPK / ERK Inactivation
Yao, Z., & Seger, R. (2004) · Current Genomics · doi:10.2174/1389202043349309 · Cited by 32 · see citing works
Poddar, R., Rajagopal, S., Shuttleworth, C. W., & Paul, S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.663468 · Cited by 29 · see citing works
Striatal-Enriched Protein Tyrosine Phosphatase in Alzheimer’s Disease
Xu, J., Kurup, P. K., Nairn, A. C., & Lombroso, P. J. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-394816-8.00009-x · Cited by 29 · see citing works
“p38 is a second member of the MAPK family that is dephosphorylated and inactivated by STEP (Munoz et al., 2003; Poddar et al., 2010; Xu et al., 2009).”
BackgroundThe STEP 61 interactome reveals subunit-specific AMPA receptor binding and synaptic regulation
Won, S., Incontro, S., Li, Y., Nicoll, R. A., & Roche, K. W. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900878116 · Cited by 29 · see citing works
“The middle region of STEP61, including the kinase-interacting motif (KIM) and kinase-specificity sequence (KIS) domains (45), is important for its binding to the GluA2 C-terminal region (Fig.”
BackgroundLorber, B., Berry, M., Hendriks, W. J. A. J., den Hertog, J., Pulido, R., & Logan, A. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.06.012 · Cited by 29 · see citing works
“Concentrations of the antibodies used were as follows: polyclonal rabbit anti-STEP 1– 369 (Munoz et al., 2003), used at 1/1600 on ON and eye sections; polyclonal rabbit anti-LAR (Schaapveld, 1997), used at 1/2500 on ON, and at 1/3000 on eye sections; polyclonal rabbit anti-RPTPa 5478 (Den Hertog et al.”
BackgroundMethodInfluentialSelf-citationStructural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase,
Critton, D. A., Tortajada, A., Stetson, G., Peti, W., & Page, R. (2008) · Biochemistry · doi:10.1021/bi801724n · Cited by 28 · see citing works
Bardwell, A. J., & Bardwell, L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691436 · Cited by 27 · see citing works
Witten, M. R., Wissler, L., Snow, M., Geschwindner, S., Read, J. A., Brandon, N. J., Nairn, A. C., Lombroso, P. J., Käck, H., & Ellman, J. A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01292 · Cited by 29 · see citing works
Developmental localization of NMDA receptors, Src and MAP kinases in mouse brain
Jiang, X., Knox, R. N., Pathipati, P., & Ferriero, D. M. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.08.039 · Cited by 27 · see citing works
“By contrast, the striatal-enriched tyrosine phosphatase (STEP) dephosphorylates NR2B at Y1472 and reduces activity of its substrates ERK and p38 [1, 13, 15].”
BackgroundTashev, R. E., de Moura, P. J., Venkitaramani, D. V., Prosperetti, C., Centonze, D., Paul, S., & Lombroso, P. J. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.10.008 · Cited by 27 · see citing works
“Previous studies have shown that STEP limits the duration of ERK1/2 activation and downstream transcriptional responses following glutamate receptor stimulation (30,31).”
BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome
Saavedra, A., Puigdellívol, M., Tyebji, S., Kurup, P. K., Xu, J., Ginés, S., Alberch, J., Lombroso, P. J., & Pérez‐Navarro, E. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9335-7 · Cited by 24 · see citing works
“(NMDA) glutamate receptor subunit GluN2B [18, 19] and extracellular signal-regulated kinase 1/2 (ERK1/2) [20, 21].”
BackgroundTárrega, C., Ríos, P., Cejudo-Marín, R., Blanco‐Aparicio, C., van den Berk, L., Schepens, J. T. G., Hendriks, W. J. A. J., Tabernero, L., & Pulido, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504366200 · Cited by 25 · see citing works
Self-citationThe interaction of p38 with its upstream kinase MKK6
Kumar, G. S., Page, R., & Peti, W. (2021) · Protein Science · doi:10.1002/pro.4039 · Cited by 24 · see citing works
“3–5 Dephosphorylation by different downstream phosphatases, including the KIMprotein tyrosine phosphatases (KIM-PTPs), leads to p38 inactivation.(6,7) Phosphatases, MAPKKs and substrates bind to p38 using short linear motifs (SLiMs) known as D-motifs or Kinase Interaction Motifs (KIM).”
BackgroundMachado, L. E. S. F., Shen, T., Page, R., & Peti, W. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.774174 · Cited by 24 · see citing works
Mukherjee, S., Poddar, R., Deb, I., & Paul, S. (2011) · Biochemical Journal · doi:10.1042/bj20110240 · Cited by 24 · see citing works
Tolleson, M. W., Gill, C. A., Herring, A. D., Riggs, P. K., Sawyer, J. E., Sanders, J. O., & Riley, D. G. (2017) · Journal of Animal Science · doi:10.2527/jas.2017.1475 · Cited by 22 · see citing works
Tjin, C. C., Otley, K. D., Baguley, T. D., Kurup, P. K., Xu, J., Nairn, A. C., Lombroso, P. J., & Ellman, J. A. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00486 · Cited by 22 · see citing works
Mahaman, Y. A. R., Huang, F., Embaye, K. S., Wang, X., & Zhu, F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.680118 · Cited by 22 · see citing works
“Other molecules that are involved in synaptic plasticity and memory, and have also been confirmed substrates of STEP are the two members of the MAPK family ERK1/2 and p38 (Muñoz et al., 2003; Paul et al., 2003; Kim et al., 2008; Paul and Connor, 2010).”
BackgroundSTEP regulation of seizure thresholds in the hippocampus
Briggs, S. W., Walker, J., Asik, K., Lombroso, P. J., Naegele, J. R., & Aaron, G. B. (2011) · Epilepsia · doi:10.1111/j.1528-1167.2010.02912.x · Cited by 22 · see citing works
“STEP dephosphorylates and inactivates the key signaling molecules ERK1/2, p38, and Fyn, and has also been shown to dephosphorylate and induce internalization of the ionotropic glutamate receptors GluN1/GluN2B and GluA1/ GluA2 (Snyder et al., 2005; Zhang et al., 2008; Kurup et al., 2010a).”
BackgroundFrancis, D. M., Kumar, G. S., Koveal, D., Tortajada, A., Page, R., & Peti, W. (2013) · Structure · doi:10.1016/j.str.2013.07.003 · Cited by 21 · see citing works
Klassert, T. E., Bräuer, J., Hölzer, M., Stock, M., Riege, K., Zubiría-Barrera, C., Müller, M. M., Rummler, S., Skerka, C., Marz, M., et al. (2017) · Scientific Reports · doi:10.1038/srep40599 · Cited by 20 · see citing works
“These included PTPN7, DUSP1 and DUSP7, which have shown to regulate the MAPK signaling pathway 60,61 .”
Docking Interactions of Hematopoietic Tyrosine Phosphatase with MAP Kinases ERK2 and p38α
Piserchio, A., Francis, D. M., Koveal, D., Dalby, K. N., Page, R., Peti, W., & Ghose, R. (2012) · Biochemistry · doi:10.1021/bi3012725 · Cited by 19 · see citing works
Lombroso, P. J., Ogren, M. P., Kurup, P. K., & Nairn, A. C. (2016) · F1000Research · doi:10.12688/f1000research.8571.1 · Cited by 19 · see citing works
Carvajal, F. J., & Cerpa, W. F. (2021) · Antioxidants · doi:10.3390/antiox10101575 · Cited by 20 · see citing works
“The dose used had already been previously reported [29,51], but in any case, we evaluated the effectiveness of the treatment through a known target of STEP61 phosphatase activity, which is the phosphorylation of ERK [52,53].”
BackgroundMethodPalacios, L., Dickinson, R. J., Sacristán-Reviriego, A., Didmon, M. P., Marín, M. J., Martı́n, H., Keyse, S. M., & Molina, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.286948 · Cited by 19 · see citing works
Shi, C., Zhang, K., & Xu, Q. (2011) · Journal of Affective Disorders · doi:10.1016/j.jad.2011.10.026 · Cited by 18 · see citing works
Tyrosine-specific MAPK phosphatases and the control of ERK signaling in PC12 cells
Noordman, Y. E., Jansen, P. A. M., & Hendriks, W. J. A. J. (2006) · Journal of Molecular Signaling · doi:10.1186/1750-2187-1-4 · Cited by 18 · see citing works
“In line with our findings, ectopic overexpression of a cytosolic version of PTP-SL (thus resembling PTPPBSγ isoforms) in PC12 cells has been reported previously to result in reduced phospho-ERK5 and phospho-ERK1/2 levels following EGF administration [27].”
BackgroundWang, Q., Xu, C., Cai, R., An, W., Yuan, H., & Xu, M. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13290 · Cited by 18 · see citing works
Masuda, K., Katagiri, C., Nomura, M., Sato, M., Kakumoto, K., Akagi, T., Kikuchi, K., Tanuma, N., & Shima, H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.097 · Cited by 17 · see citing works
Sood, R. F., Arbabi, S., Honari, S. E., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0149206 · Cited by 17 · see citing works
“Three main classes of MAPKs in humans include the extracellular signal-regulated kinases (ERKs), c-Jun N-terminal kinases (JNKs), and p38 kinases, each of which is rapidly activated by sequential phosphorylation steps by specific upstream MAPK kinases [8].”
BackgroundHe, R.-B., Li, L., Liu, L.-Z., Ma, Y.-J., Fan, S., Liu, L.-R., Li, W.-B., & Xian, X. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15874 · Cited by 13 · see citing works
“Similarly, STEP61 cleavage increases p38 MAPK phosphorylation at the Tyr182 site, thereby activating the p38 MAPK (Muñoz et al., 2003).”
BackgroundFrancis, D. M., Koveal, D., Tortajada, A., Page, R., & Peti, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091934 · Cited by 16 · see citing works
“We also tested peptides that include the kinase specificity sequence (KIS) regions, as we [14,15] and others [12] have shown that KIS residues can interact directly with ERK2 and p38a.”
MethodLee, Z.-F., Huang, T.-H., Chen, S., & Cheng, I. H.-J. (2021) · Pain · doi:10.1097/j.pain.0000000000002180 · Cited by 15 · see citing works
Lambert, L. J., Grotegut, S., Celeridad, M., Gosalia, P., Backer, L. J. S. D., Bobkov, A. A., Salaniwal, S., Chung, T. D. Y., Zeng, F., Pass, I., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094417 · Cited by 14 · see citing works
“Known STEP substrates include the mitogen-activated protein kinase (MAPK) family members extracellular signal-regulated kinases 1/2 (ERK1/2) and p38 [21,22], the tyrosine kina es F n and Pyk2 [23,24], the glutamate receptor GluN2B subunit (also known as NR2B) of N-methyl-D-aspartate (NMDA) receptors [25–27], and the G…”
BackgroundMoskaliuk, V. S., Kozhemyakina, R. V., Базовкина, Д. В., Terenina, E. E., Khomenko, T. M., Volcho, K. P., Salakhutdinov, N. F., Kulikov, A. V., Naumenko, V. S., & Kulikova, E. A. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112667 · Cited by 15 · see citing works
Behavioral characterization of striatal‐enriched protein tyrosine phosphatase ( STEP ) knockout mice
Rizzo, S. J. S., Lotarski, S. M., Stolyar, P., et al. (2014) · Genes Brain & Behavior · doi:10.1111/gbb.12169 · Cited by 13 · see citing works
“STEP has also been shown to dephosphorylate and inactivate multiple kinases, including Fyn (Nguyen et al. 2002), Pyk2 (Xu et al. 2012) and mitogen-activated protein kinases (MAPKs), ERK1/2 and p38 (Munoz et al. 2003; Paul et al. 2003).”
BackgroundNoordman, Y. E., Augustus, E. D., Schepens, J. T. G., Chirivi, R. G. S., Ríos, P., Pulido, R., & Hendriks, W. J. A. J. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.023 · Cited by 13 · see citing works
Self-citationFunctional assignment of MAPK phosphatase domains
Nordle, A. K. L., Ríos, P., Gaulton, A., Pulido, R., Attwood, T. K., & Tabernero, L. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21477 · Cited by 13 · see citing works
Self-citationReinhart, V., Nguyen, T., Gerwien, R. W., et al. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.08.002 · Cited by 12 · see citing works
“…receptor subtype 2B (NR2B) subunit of the NMDA receptor (Braithwaite et al., 2006), as well as several kinases: FYN (Nguyen et al., 2002), PYK2 (Xu et al., 2012), and mitogen-activated protein kinases extracellular signal-regulated kinase (ERK1/2) and p38 (Munoz et al., 2003; Paul et al., 2003).”
Synaptic NMDA Receptor Activation Induces Ubiquitination and Degradation of STEP61
Xu, J., Kurup, P. K., Nairn, A. C., & Lombroso, P. J. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0555-x · Cited by 12 · see citing works
Interface Analysis of the Complex between ERK2 and PTP-SL
Balasu, M. C., Spiridon, L. N., Miron, S. M., Craescu, C. T., Scheidig, A. J., Petrescu, A., & Szedlacsek, S. E. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005432 · Cited by 12 · see citing works
“Thus, PTP-SL preferentially binds ERK1/2 whereas STEP and HePTP selectively bind p38a [7].”
BackgroundCheng, R., Tang, M., Martinez, I. M., Ayodele, T., Baez, P., Reyes‐Dumeyer, D., Lantigua, R., Medrano, M. Z., Jiménez‐Velázquez, I. Z., Lee, J. H., et al. (2018) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2018.07.007 · Cited by 11 · see citing works
A PTP4A3 Peptide PIMAP39 Modulates TNF-Alpha Levels and Endotoxic Shock
Tang, X., Woodward, T. A., & Amar, S. (2009) · Journal of Innate Immunity · doi:10.1159/000235685 · Cited by 11 · see citing works
Francis, D. M., Page, R., & Peti, W. (2013) · Biomolecular NMR Assignments · doi:10.1007/s12104-013-9480-8 · Cited by 8 · see citing works
Non-transmembrane PTPs in Cancer
Hendriks, W. J. A. J., & Böhmer, F. (2016) · Springer eBooks · doi:10.1007/978-1-4939-3649-6_3 · Cited by 8 · see citing works
Erkens, M., Bakker, B., van Duijn, L. M., Hendriks, W. J. A. J., & der Zee, C. E. E. M. V. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.02.014 · Cited by 6 · see citing works
Don’t Take Away My P: Phosphatases as Therapeutic Targets in Huntington’s Disease
Saavedra, A., Alberch, J., & Pérez‐Navarro, E. (2012) · InTech eBooks · doi:10.5772/30850 · Cited by 6 · see citing works
Uncovering the Significance of STEP61 in Alzheimer’s Disease: Structure, Substrates, and Interactome
Bagwe, P. V., Deshpande, R. D., Juhász, G., Sathaye, S. S., & Joshi, S. V. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01364-2 · Cited by 5 · see citing works
Walters, J. M., Noblet, H. A., & Chung, H. J. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106641 · Cited by 5 · see citing works
“Both STEP 46 and STEP 61 regulate two members of the mitogen-activated protein kinase family, including ERK1/2 and p38 (Munoz et al., 2003; Paul et al., 2003; Poddar et al., 2010; Pulido et al., 1998).”
BackgroundDual-action kinase inhibitors influence p38α MAP kinase dephosphorylation
Stadnicki, E. J., Ludewig, H., Kumar, R. P., Wang, X., Qiao, Y., Kern, D., & Bradshaw, N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2415150122 · Cited by 4 · see citing works
“…is controlled by upstream kinases, autophosphorylation, and a suite of protein phosphatases ( 26 ), including serine/threonine phosphatases WIP1 ( 15 , 30 , 31 ), PPM1A ( 32 ), and PP2A ( 33 – 36 ) as well as tyrosine phosphatases (PTPs) ( 37 ), and dual - specificity phosphatases (DUSPs) ( 38 ).”
Rajagopal, S., Poddar, R., & Paul, S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100944 · Cited by 5 · see citing works
Machado, L. E. S. F., Page, R., & Peti, W. (2017) · Biomolecular NMR Assignments · doi:10.1007/s12104-017-9770-7 · Cited by 4 · see citing works
“It functions to negatively regulate T cell activation and proliferation through its ability to dephosphorylate and inactivate the MAP kinases p38 and Erk2 (Muñoz et al. 2003; Francis et al. 2011).”
Hendriks, W. J. A. J., van Cruchten, R. T. P., & Pulido, R. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1051311 · Cited by 4 · see citing works
Self-citation
- Authors
- MUÑOZ, J. J., TÁRREGA, C., BLANCO-APARICIO, C., & PULIDO, R.
- Affiliations
- The Instituto de Investigaciones Citológicas, Amadeo de Saboya, 4, 46010 Valencia, Spain
- ORCID
- PULIDO, Rafael
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2003-05-15
- Volume
- 372
- Issue
- 1
- Pages
- 193-201
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1223371
- OpenAlex
- W2038679488
- Semantic Scholar
- b8fb7a2ea61d532afaae5b320f42cabe6985ee06
- Cited by
- 121
- References
- 53
- Citations by year
- 2026: 5 · 2024: 6 · 2023: 3 · 2022: 2 · 2021: 6 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 10 · 2016: 7 · 2015: 6 · 2014: 5 · 2013: 8 · 2012: 10
- FWCI
- 1.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission (HPRN-CT-2000-00085)
- Ministerio de Ciencia y Tecnología
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- protein tyrosine phosphatase, STEP, ERK1/2, p38α, mitogen-activated protein kinase, reducing agents, redox regulation, protein-protein interaction, nuclear translocation
- MeSH terms
- Animals, Cell Nucleus, Humans, Substrate Specificity, Protein Tyrosine Phosphatases, Reducing Agents, COS Cells, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, Protein Transport, p38 Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase 3
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