Cited by 1,369Protein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancerCancer Mechanisms and Therapy

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The specificities of protein kinase inhibitors: an update

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BAIN, Jenny, McLAUCHLAN, Hilary, ELLIOTT, Matthew, COHEN, Philip·2003·Biochemical Journal

DOI 10.1042/bj20021535PMC PMC1223271

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Abstract

We have previously examined the specificities of 28 commercially available compounds, reported to be relatively selective inhibitors of particular serine/threonine-specific protein kinases [Davies, Reddy, Caivano and Cohen (2000) Biochem. J. 351, 95—105]. In the present study, we have extended this analysis to a further 14 compounds. Of these, indirubin-3′-monoxime, SP 600125, KT 5823 and ML-9 were found to inhibit a number of protein kinases and conclusions drawn from their use in cell-based assays are likely to be erroneous. Kenpaullone, Alsterpaullone, Purvalanol, Roscovitine, pyrazolopyrimidine 1 (PP1), PP2 and ML-7 were more specific, but still inhibited two or more protein kinases with similar potency. Our results suggest that the combined use of Roscovitine and Kenpaullone may be useful for identifying substrates and physiological roles of cyclin-dependent protein kinases, whereas the combined use of Kenpaullone and LiCl may be useful for identifying substrates and physiological roles of glycogen synthase kinase 3. The combined use of SU 6656 and either PP1 or PP2 may be useful for identifying substrates of Src family members. Epigallocatechin 3-gallate, one of the main polyphenolic constituents of tea, inhibited two of the 28 protein kinases in the panel, dual-specificity, tyrosine-phosphorylated and regulated kinase 1A (DYRK1A; IC50 = 0.33μM) and p38-regulated/activated kinase (PRAK; IC50 = 1.0μM).

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Background
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Background
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Background
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Background
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Background
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Background
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“We followed the recommendations of Davies et al. (2000) and Bain et al. (2003) for the use of protein kinase inhibitors in cell-based assays when we designed our experiments to ensure that the concentrations of the inhibitors used (CK1-7 and IC261) are selective for CK1.”
Method
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Bauerle, K. T., Schweppe, R. E., & Haugen, B. R. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-117 · Cited by 59
“In our studies, however, treatment with the JNK inhibitor, SP600125, alone inhibited growth of our thyroid cancer cell lines (data not shown), likely due to off-target mechanisms associated with the compound, as described by Bain and colleagues [38].”
Influence of prenatal EGCG treatment andDyrk1adosage reduction on craniofacial features associated with Down syndrome
McElyea, S. D., Starbuck, J. M., Tumbleson, D. M., Harrington, E., Blazek, J. D., Ghoneima, A. A. M., Kula, K. S., & Roper, R. J. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw309 · Cited by 55
Development of Selective Clk1 and -4 Inhibitors for Cellular Depletion of Cancer-Relevant Proteins
ElHady, A. K., Abdel‐Halim, M., Abadi, A., & Engel, M. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01915 · Cited by 59
Prenatal treatment with EGCG enriched green tea extract rescues GAD67 related developmental and cognitive defects in Down syndrome mouse models
Souchet, B., Duchon, A., Gu, Y., Dairou, J., Chevalier, C., Daubigney, F., Nalesso, V., Créau, N., Yu, Y., Janel, N., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40328-9 · Cited by 54
Synthesis and Biological Validation of a Harmine-Based, Central Nervous System (CNS)-Avoidant, Selective, Human β-Cell Regenerative Dual-Specificity Tyrosine Phosphorylation-Regulated Kinase A (DYRK1A) Inhibitor
Kumar, K., Wang, P., Wilson, J., Zlatanic, V., Berrouet, C. C., Khamrui, S., Secor, C., Swartz, E., Lazarus, M. B., Sánchez, R., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01379 · Cited by 60
Inhibition of myosin light chain phosphorylation decreases rat mesenteric lymphatic contractile activity
Wang, W., Nepiyushchikh, Z., Zawieja, D. C., Chakraborty, S., Zawieja, S. D., Gashev, A. A., Davis, M. J., & Muthuchamy, M. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00312.2009 · Cited by 64
“We did not use higher doses of ML-7 (10 (4)M) to keep the pharmacological level of ML-7 in the range that has been reported to be relatively selective for MLCK inhibition (3).”
Background
Rescue of the abnormal skeletal phenotype in Ts65Dn Down syndrome mice using genetic and therapeutic modulation of trisomicDyrk1a
Blazek, J. D., Abeysekera, I., Li, J., & Roper, R. J. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv284 · Cited by 57
“To determine whether the known DYRK1A inhibitor EGCG (22) could improve the BMD and structural deficits observed in the Ts65Dn skeleton, we treated 3-week-old Ts65Dn and euploid mice with EGCG (∼9 mg/kg/day) or water for 3 weeks.”
Method
Protein tyrosine kinase signaling during oocyte maturation and fertilization
McGinnis, L. K., Carroll, D. J., & Kinsey, W. H. (2011) · Molecular Reproduction and Development · doi:10.1002/mrd.21326 · Cited by 58
“…the catalytic activity yet cannot distinguish among SRC-family members, do not block scaffolding functions, and usually exhibit inhibitory activity against the ABL kinase family at the concentrations commonly used (Hanke et al., 1996; Blake et al., 2000; Bain et al., 2003;Golaset al., 2005).”
Background
Can MM‐PBSA calculations predict the specificities of protein kinase inhibitors?
Page, C. S., & Bates, P. A. (2006) · Journal of Computational Chemistry · doi:10.1002/jcc.20534 · Cited by 58
Regulation of RANTES/CCL5 expression in human astrocytes by interleukin‐1 and interferon‐β
Kim, M., Suh, H.-S., Brosnan, C. F., & Lee, S. C. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02487.x · Cited by 58
“However, the specific role of p38 and JNK MAPKs in the induction of astrocyte RANTES gene remains to be determined.”
BackgroundInfluential
Second-generation kinase inhibitors
Klebl, B., & Müller, G. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.5.975 · Cited by 59
“The selectivity panels consisting of in vitro kinase activity assays [16,18] have grown larger and new chemoproteomic technologies have been developed, which”
BackgroundMethod
Lyn-mediated SHP-1 recruitment to CD5 contributes to resistance to apoptosis of B-cell chronic lymphocytic leukemia cells
Tibaldi, E. V., Brunati, A. M., Zonta, F., Frezzato, F., Gattazzo, C., Zambello, R., Gringeri, E., Semenzato, G., Pagano, M. A., & Trentin, L. (2011) · Leukemia · doi:10.1038/leu.2011.152 · Cited by 57
SP600125 suppresses Cdk1 and induces endoreplication directly from G2 phase, independent of JNK inhibition
Kim, J. A., Lee, J.-S., Margolis, R. L., & Fotedar, R. (2010) · Oncogene · doi:10.1038/onc.2009.464 · Cited by 57
“We conclude that SP600125 is not a specific inhibitor of JNK inhibition in accord with Bain et al. (2003, 2007).”
BackgroundResult
Tsc2 Is a Molecular Checkpoint Controlling Osteoblast Development and Glucose Homeostasis
Riddle, R. C., Frey, J. L., Tomlinson, R. E., Ferron, M., Li, Y., DiGirolamo, D. J., Monier‐Faugere, M., Hussain, M. A., Karsenty, G., & Clemens, T. L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00075-14 · Cited by 57
“Application of SP600125, a synthetic inhibitor of Jnk and also of S6K1 (31), to inhibit this pathway and prevent the targeting of Irs1 for degradation (32, 33) normalized Irs-1 protein levels (Fig.”
Background
Inhibition of the Cyclin-Dependent Kinases at the Beginning of Human Cytomegalovirus Infection Specifically Alters the Levels and Localization of the RNA Polymerase II Carboxyl-Terminal Domain Kinases cdk9 and cdk7 at the Viral Transcriptosome
Kapasi, A. J., & Spector, D. H. (2007) · Journal of Virology · doi:10.1128/jvi.01681-07 · Cited by 57
Localized activation of Src-family protein kinases in the mouse egg
McGinnis, L. K., Albertini, D. F., & Kinsey, W. H. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2007.03.024 · Cited by 57
“The Src-family PTK inhibitor PP2 had a small, but significant effect on zygote development at concentrations between 10 and 100 μM, a range at which it could have non-specific effects on other protein kinases (Tatton et al., 2003; Bain et al., 2003).”
Background
Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery
Takizawa, N., Ikebe, R., Ikebe, M., & Luna, E. J. (2007) · Journal of Cell Science · doi:10.1242/jcs.008219 · Cited by 57
“, 2003); by ML-7 at a concentration (1 M) that specifically inhibits MLCK (Bain et al., 2003); and by the drug U0126, an indirect inhibitor of MLCK via the upstream kinase MEK (Fincham et al.”
Background
Attenuation of Ozone-Induced Airway Inflammation and Hyper-Responsiveness by c-Jun NH2 Terminal Kinase Inhibitor SP600125
Williams, A. S., Issa, R., Leung, S. Y., Nath, P., Ferguson, G. D., Bennett, B. L., Adcock, I. M., & Chung, K. F. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.121624 · Cited by 57
“We have not addressed the issue of selectivity of SP600125 in this study, an issue that was raised by a study of SP600125 on enzymatic actions of many related kinases (Bain et al., 2003).”
Background
Serine phosphorylation differentially affects RhoA binding to effectors: Implications to NGF-induced neurite outgrowth
Nusser, N., Gosmanova, E., Makarova, N., Fujiwara, Y., Yang, L., Guo, F., Luo, Y., Zheng, Y., & Tigyi, G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.06.010 · Cited by 57
Wnt‐3a and Wnt‐3 differently stimulate proliferation and neurogenesis of spinal neural precursors and promote neurite outgrowth by canonical signaling
David, M. D., Cantı́, C., & Herreros, J. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22464 · Cited by 56
“SCNP-derived neurons treated with the selective GSK-3b inhibitor BIO (Sato et al., 2004) or kenpaullone, which inhibits GSK-3b, Cdks, and other kinases (Bain et al., 2003), from 2 DIV to 3 DIV showed an increased total neurite length of 23% and 26%, respectively, compared with control (Fig.”
Geldanamycin-induced Lyn dissociation from aberrant Hsp90-stabilized cytosolic complex is an early event in apoptotic mechanisms in B-chronic lymphocytic leukemia
Trentin, L., Frasson, M., Donella‐Deana, A., Frezzato, F., Pagano, M. A., Tibaldi, E. V., Gattazzo, C., Zambello, R., Semenzato, G., & Brunati, A. M. (2008) · Blood · doi:10.1182/blood-2008-02-139139 · Cited by 57
Kinetic Properties of a MNB/DYRK1A Mutant Suitable for the Elucidation of Biochemical Pathways
Adayev, T., Chen‐Hwang, M., Murakami, N., Węgiel, J., & Hwang, Y. (2006) · Biochemistry · doi:10.1021/bi060632j · Cited by 56
Wnt5a Signaling in Normal and Cancer Stem Cells
Zhou, Y., Kipps, T. J., & Zhang, S. (2017) · Stem Cells International · doi:10.1155/2017/5295286 · Cited by 62
“The first evidence for this was provided by a study of a pharmacological inhibitor of glycogen synthase kinase-3 (GSK3) that could modulate GSK3 activity, leading to activation of β-catenin canonical signaling and increased stability of c-Myc [25, 26].”
Background
N-&-N, a new class of cell death-inducing kinase inhibitors derived from the purine roscovitine
Bettayeb, K., Sallam, H., Ferandin, Y., Popowycz, F., Fournet, G., Hassan, M., Echalier, A., Bernard, P., Endicott, J., Joseph, B., et al. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0080 · Cited by 56
Mechanical Tension Promotes the Osteogenic Differentiation of Rat Tendon-derived Stem Cells Through the Wnt5a/Wnt5b/JNK Signaling Pathway
Liu, X., Chen, W., Zhou, Y. L., Tang, K., & Zhang, J. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000430117 · Cited by 56
GPCR ‐mediated EGF receptor transactivation regulates TRPV 4 action in the vasculature
Saifeddine, M., El‐Daly, M., Mihara, K., Bunnett, N. W., McIntyre, P., Altier, C., Hollenberg, M. D., & Ramachandran, R. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13072 · Cited by 53
“, 2014) and fully took into account recommended guidelines for judicious use of pharmacological inhibitors of signalling protein function (Bain et al., 2003; 2007; Cohen, 2010).”
Background
Ligand release-independent transactivation of epidermal growth factor receptor by transforming growth factor-β involves multiple signaling pathways
Joo, C.-K., Kim, H. S., Park, J.-Y., Seomun, Y., Son, M.-J., & Kim, J.-T. (2007) · Oncogene · doi:10.1038/sj.onc.1210649 · Cited by 55
Thrombin Induces Fibroblast CCL2/JE Production and Release via Coupling of PAR1to Gαqand Cooperation between ERK1/2 and Rho Kinase Signaling Pathways
Deng, X., Mercer, P. F., Scotton, C. J., Gilchrist, A., & Chambers, R. C. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-07-0720 · Cited by 56
“In this study, all experiments involving such inhibitors were designed according to expert recommendations (Davies et al., 2000; Bain et al., 2003).”
Method
Inhibition of RET tyrosine kinase by SU5416
Mologni, L., Sala, E., Cazzaniga, S., Rostagno, R., Kuoni, T., Puttini, M., Bain, J., Cleris, L., Redaelli, S., Riva, B., et al. (2006) · Journal of Molecular Endocrinology · doi:10.1677/jme.1.01999 · Cited by 58
“Procedures for purification and assay of 30 of the 52 kinases have been described (Davies et al. 2000, Bain et al. 2003).”
MethodSelf-citation
Contribution of UVB and UVA to UV-dependent stimulation of cyclooxygenase-2 expression in artificial epidermis
Mahns, A., Wolber, R., Stäb, F., Klotz, L., & Sies, H. (2004) · Photochemical & Photobiological Sciences · doi:10.1039/b309067a · Cited by 55
Effects of tumour necrosis factor α (TNFα) on Mytilus haemocytes: role of stress‐activated mitogen‐activated protein kinases (MAPKs)
Betti, M., Ciacci, C., Lorusso, L. C., Canonico, B., Falcioni, T., Gallo, G., & Canesi, L. (2006) · Biology of the Cell · doi:10.1042/bc20050049 · Cited by 55
“However, SP600125, the most widely utilized JNK inhibitor in mammalian cells, has been criticized for its low specificity towards JNK isoforms (Bain et al., 2003), and particular care must be taken in interpreting the results obtained with JNK inhibitors, in both vertebrate and invertebrate systems.”
Background
Identification of glycogen synthase as a new substrate for stress-activated protein kinase 2b/p38beta
Kuma, Y., Campbell, D. G., & Cuenda, A. (2004) · Biochemical Journal · doi:10.1042/bj20031559 · Cited by 55
Comparing Immobilized Kinase Inhibitors and Covalent ATP Probes for Proteomic Profiling of Kinase Expression and Drug Selectivity
Lemeer, S., Zörgiebel, C., Ruprecht, B., Kohl, K., & Küster, B. (2013) · Journal of Proteome Research · doi:10.1021/pr301073j · Cited by 57
Flavanoids induce expression of the suppressor of cytokine signalling 3 (SOCS3) gene and suppress IL-6-activated signal transducer and activator of transcription 3 (STAT3) activation in vascular endothelial cells
Wiejak, J., Dunlop, J., Mackay, S. P., & Yarwood, S. J. (2013) · Biochemical Journal · doi:10.1042/bj20130481 · Cited by 55
Triterpenoid saponin, oleanolic acid 3-O-β-d-glucopyranosyl(1→3)-α-l-rhamnopyranosyl(1→2)-α-l-arabinopyranoside (OA) from Aralia elata inhibits LPS-induced nitric oxide production by down-regulated NF-κB in raw 264.7 cells
Suh, S., Jin, U., Kim, K., Son, J., Lee, S. H., Son, K.-H., Chang, H. W., Lee, Y., & Kim, C. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.08.025 · Cited by 54
Pharmacological interventions to improve cognition and adaptive functioning in down syndrome: strides to date.
Hart, S. J., Visootsak, J., Tamburri, P., Phuong, P., Baumer, N., Hernandez, M., Skotko, B. G., Ochoa‐Lubinoff, C., Liogier D'Ardhuy, X., Kishnani, P. S., et al. (2017) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.38465 · Cited by 54
DYRK1A kinase inhibition with emphasis on neurodegeneration: A comprehensive evolution story-cum-perspective
Pathak, A., Rohilla, A., Gupta, T., Akhtar, M. J., Haider, M. R., Sharma, K., Haider, K., & Yar, M. S. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.093 · Cited by 56
Computational chemistry approach to protein kinase recognition using 3D stochastic van der Waals spectral moments
González‐Díaz, H., Saı́z-Urra, L., Molina, R., González‐Díaz, Y., & González, A. S. (2007) · Journal of Computational Chemistry · doi:10.1002/jcc.20649 · Cited by 54
Cell growth, global phosphotyrosine elevation, and c-Met phosphorylation through Src family kinases in colorectal cancer cells
Emaduddin, M., Bicknell, D. C., Bodmer, W. F., & Feller, S. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712176105 · Cited by 50
“To address this issue, 16 CRC lines with either very high- or low-SFK activity were selected and exposed to different doses of PP2, a well characterized SFK inhibitor with a good selectivity profile (17).”
Method
Targeting c-Jun and JunB proteins as potential anticancer cell therapy
Gurzov, E. N., Bakiri, L., Alfaro, J. M., Wagner, E. F., & Izquierdo, M. (2007) · Oncogene · doi:10.1038/sj.onc.1210690 · Cited by 53
“Despite its controversial specificity (Bennett et al., 2001; Bain et al., 2003), SP600125 appears as a novel JNK/c-Jun inhibitor with a real potential for cancer treatment (Mingo-Sion et al.”
Background
Transforming Growth Factor-β1 (TGFβ1) Stimulates Connective Tissue Growth Factor (CCN2/CTGF) Expression in Human Gingival Fibroblasts through a RhoA-independent, Rac1/Cdc42-dependent Mechanism
Black, S. A., & Trackman, P. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710363200 · Cited by 53
Implications for selectivity of 3,4-diarylquinolinones as p38αMAP kinase inhibitors
Peifer, C., Urich, R., Schattel, V., Abadleh, M. M., Röttig, M., Kohlbacher, O., & Laufer, S. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.12.073 · Cited by 53
Pyrvinium pamoate does not activate protein kinase CK1, but promotes Akt/PKB down-regulation and GSK3 activation
Venerando, A., Girardi, C., Ruzzene, M., & Pinna, L. A. (2013) · Biochemical Journal · doi:10.1042/bj20121140 · Cited by 51
Activation of Adenosine A2A Receptors Induces TrkB Translocation and Increases BDNF-Mediated Phospho-TrkB Localization in Lipid Rafts: Implications for Neuromodulation
Assaife‐Lopes, N., Sousa, V. C., Pereira, D. B., Ribeiro, J. A., Chao, M. V., & Sebastião, A. M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5695-09.2010 · Cited by 53
“5 M) (Bain et al., 2003) on CGS 21680-induced TrkB translocation to lipid rafts.”
Influential
Retracted
JNK activation is essential for activation of MEK/ERK signaling in IL-1β-induced COX-2 expression in synovial fibroblasts
Kitanaka, T., Nakano, R., Kitanaka, N., Kimura, T., Okabayashi, K., Narita, T., & Sugiya, H. (2017) · Scientific Reports · doi:10.1038/srep39914 · Cited by 53
Platelet MAPKs—a 20+ year history: What do we really know?
Patel, P., & Naik, U. P. (2020) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.14967 · Cited by 56

Authors: BAIN, J., McLAUCHLAN, H., ELLIOTT, M., & COHEN, P.
Affiliations: University of Dundee (GB)
Corresponding author: BAIN, Jenny
McLAUCHLAN, Hilary
ELLIOTT, Matthew
COHEN, Philip
ORCID: ELLIOTT, Matthew
COHEN, Philip
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2003-04-01
Volume: 371
Issue: 1
Pages: 199-204
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20021535
PMC: PMC1223271
OpenAlex: W2011588737
Cited by: 1,369
References: 42
Citations by year: 2026: 9 · 2025: 21 · 2024: 12 · 2023: 16 · 2022: 26 · 2021: 35 · 2020: 28 · 2019: 38 · 2018: 42 · 2017: 48 · 2016: 42 · 2015: 44 · 2014: 52 · 2013: 66 · 2012: 70
FWCI: 43.75
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
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 › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
Keywords: protein kinase inhibitors, kinase selectivity, serine/threonine kinase, indirubin-3'-monoxime, KT5823, ML-9, kenpaullone, roscovitine, pyrazolopyrimidines, cyclin-dependent kinases, glycogen synthase kinase-3, Src family kinases, epigallocatechin gallate, DYRK1A, kinase substrate identification
MeSH terms: Alkaloids, Anthracenes, Azepines, Benzazepines, Carbazoles, Catechin, Enzyme Inhibitors, Indoles, Kinetin, Naphthalenes, Oximes, Purines, Pyrazoles, Pyrimidines, Substrate Specificity, Signal Transduction, Cyclin-Dependent Kinases, src-Family Kinases, Mitogen-Activated Protein Kinases, Glycogen Synthase Kinase 3, Protein Kinase Inhibitors, JNK Mitogen-Activated Protein Kinases

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The specificities of protein kinase inhibitors: an update

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