Cited by 110Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.

The JNKK2-JNK1 Fusion Protein Acts As a Constitutively Active c-Jun Kinase That Stimulates c-Jun Transcription Activity

Open access

Zheng, Chaojun, Xiang, Jialing, Hunter, Tony, Lin, Anning·1999·Journal of Biological Chemistry

Open this paper in CoChat — free account

Abstract

c-Jun N-terminal protein kinase (JNK), a member of the mitogen-activated protein (MAP) kinase family, regulates gene expression in response to various extracellular stimuli. JNK is activated by JNK-activating kinase (JNKK1 and JNKK2), a subfamily of the dual specificity MAP kinase kinase (MEK) family, through phosphorylation on threonine (Thr) 183 and tyrosine (Tyr) 185 residues. The physiological functions of the JNK pathway, however, are not completely understood. A major obstacle is the lack of specific and activated kinase components that can stimulate the JNK pathway in the absence of any stimulus. Here we show that fusion of JNK1 to its upstream activator JNKK2 resulted in its constitutive activation. In HeLa cells, the JNKK2-JNK1 fusion protein showed significant JNK activity, which was comparable with that of JNK1 activated by many stimuli and activators, including EGF, TNF-alpha, anisomycin, UV irradiation, MEKK1, and small GTP binding proteins Rac1 and Cdc42Hs. Immunoblotting analysis indicated that JNK1 was phosphorylated by JNKK2 in the fusion protein on both Thr(183) and Tyr(185) residues. Like JNKK2, the JNKK2-JNK1 fusion protein was highly specific for the JNK pathway and did not activate either p38 or ERK2. Transient transfection assays demonstrated that the JNKK2-JNK1 fusion protein was sufficient to stimulate c-Jun transcriptional activity in the absence of any stimulus. Immunofluorescence analysis revealed that the JNKK2-JNK1 fusion protein was predominantly located in the nucleus of transfected HeLa cells. These results indicate that the JNKK2-JNK1 fusion protein is a constitutively active Jun kinase, which will facilitate the investigation of the physiological roles of the JNK pathway.

Integrity signals

Registry

Crossref · 10.1074/jbc.274.41.28966

Cites

60 of 60 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

We couldn’t retrieve this paper’s full text, 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?

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266
JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
A synthetic inhibitor of the mitogen-activated protein kinase cascade.
Dudley, D. T., Pang, L., Decker, S. J., Bridges, A. J., & Saltiel, A. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7686 · Cited by 2,679
The stress-activated protein kinase subfamily of c-Jun kinases
Kyriakis, J. M., Banerjee, P. T., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,601
The Regulation of AP-1 Activity by Mitogen-activated Protein Kinases
Karin, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16483 · Cited by 2,423
Induction of Apoptosis by ASK1, a Mammalian MAPKKK That Activates SAPK/JNK and p38 Signaling Pathways
Ichijo, H., Nishida, E., Irie, K., ten Dijke, P., Saitoh, M., Moriguchi, T., Takagi, M., Matsumoto, K., Miyazono, K., & Gotoh, Y. (1997) · Science · doi:10.1126/science.275.5296.90 · Cited by 2,310
Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
Cowley, S. A. (1994) · Cell · doi:10.1016/0092-8674(94)90133-3 · Cited by 1,959
Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Self-citation
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
Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms
Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Science · doi:10.1126/science.7839144 · Cited by 1,555

Flagged first, then by citations

Show all 60 references

Research works printed but not linked: 2

Minden, 1997, Biochim. Biophys. Acta, 1333, F85
Chen, 1992, Mol. Cell. Biol., 12, 915

Sorted by citations

JNK1-Mediated Phosphorylation of Bcl-2 Regulates Starvation-Induced Autophagy
Wei, Y., Pattingre, S., Sinha, S., Bassik, M., & Levine, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.001 · Cited by 1,329
Inhibition of JNK activation through NF-κB target genes
Tang, G., Minemoto, Y., Dibling, B., Purcell, N. H., Li, Z., Karin, M., & Lin, A. (2001) · Nature · doi:10.1038/35104568 · Cited by 721
Self-citation
The E3 Ubiquitin Ligase Itch Couples JNK Activation to TNFα-induced Cell Death by Inducing c-FLIPL Turnover
Chang, L., Kamata, H., Solinas, G., Luo, J.-L., Maeda, S., Venuprasad, K., Liu, Y.-C., & Karin, M. (2006) · Cell · doi:10.1016/j.cell.2006.01.021 · Cited by 706
Critical roles of c-Jun signaling in regulation of NFAT family and RANKL-regulated osteoclast differentiation
Ikeda, F., Nishimura, R., Matsubara, T., Tanaka, S., Inoue, J., Reddy, S. V., Hata, K., Yamashita, K., Hiraga, T., Watanabe, T., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419657 · Cited by 468
The Bax Subfamily of Bcl2-Related Proteins Is Essential for Apoptotic Signal Transduction by c-Jun NH 2 -Terminal Kinase
Lei, K., Nimnual, A. S., Zong, W., Kennedy, N. J., Flavell, R. A., Thompson, C. B., Bar‐Sagi, D., & Davis, R. J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4929-4942.2002 · Cited by 463
Activation of the JNK signaling pathway: Breaking the brake on apoptosis
Lin, A. (2002) · BioEssays · doi:10.1002/bies.10204 · Cited by 432
Self-citation
Ubiquitin Ligase Smurf1 Controls Osteoblast Activity and Bone Homeostasis by Targeting MEKK2 for Degradation
Yamashita, M., Ying, S., Zhang, G., Li, C., Cheng, S. Y., Deng, C., & Zhang, Y. E. (2005) · Cell · doi:10.1016/j.cell.2005.01.035 · Cited by 355
JNK1 and IKKβ: molecular links between obesity and metabolic dysfunction
Solinas, G., & Karin, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-151340 · Cited by 347
The Ubiquitin Ligase SCF Fbw7 Antagonizes Apoptotic JNK Signaling
Nateri, A. S., Riera-Sans, L., Costa, C. D., & Behrens, A. (2004) · Science · doi:10.1126/science.1092880 · Cited by 339
JNK Suppresses Apoptosis via Phosphorylation of the Proapoptotic Bcl-2 Family Protein BAD
Yu, C., Minemoto, Y., Zhang, J., Liu, J., Tang, F., Bui, T. N., Xiang, J., & Lin, A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00028-0 · Cited by 299
Self-citation
Saturated fatty acids inhibit induction of insulin gene transcription by JNK-mediated phosphorylation of insulin-receptor substrates
Solinas, G., Naugler, W., Galimi, F., Lee, M.-S., & Karin, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607626103 · Cited by 284
Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change
Gallagher, E., Gao, M., Liu, Y.-C., & Karin, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510664103 · Cited by 258
Collagen I–mediated up-regulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor 1
Shintani, Y., Fukumoto, Y., Chaika, N. V., Svoboda, R. A., Wheelock, M. J., & Johnson, K. R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708137 · Cited by 284
c-Jun N-Terminal Protein Kinase 1 (JNK1), but Not JNK2, Is Essential for Tumor Necrosis Factor Alpha-Induced c-Jun Kinase Activation and Apoptosis
Liu, J., Minemoto, Y., & Lin, A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10844-10856.2004 · Cited by 201
Self-citation
Adipocyte Fatty Acid-binding Protein Modulates Inflammatory Responses in Macrophages through a Positive Feedback Loop Involving c-Jun NH2-terminal Kinases and Activator Protein-1
Hui, X. H., Li, H., Zhou, Z., Lam, K. S. L., Xiao, Y., Wu, D., Ding, K., Wang, Y., Vanhoutte, P. M., & Xu, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.097907 · Cited by 186
Restoration of Wnt-7a Expression Reverses Non-small Cell Lung Cancer Cellular Transformation through Frizzled-9-mediated Growth Inhibition and Promotion of Cell Differentiation
Winn, R. A., Marek, L. A., Han, S., Rodriguez, K. J., Rodriguez, N., Hammond, M., Scoyk, M. M. V., Acosta, H., Mirus, J. E., Barry, N. P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409392200 · Cited by 164
Pharmacogenomic profiling of intra-tumor heterogeneity using a large organoid biobank of liver cancer
Yang, H., Cheng, J., Zhuang, H., Xu, H., Wang, Y., Zhang, T., Yang, Y., Qian, H.-G., Lu, Y., Han, F., et al. (2024) · Cancer Cell · doi:10.1016/j.ccell.2024.03.004 · Cited by 172
Activated c-Jun N-Terminal Kinase Is Required for Axon Formation
Oliva, A. A., Atkins, C. M., Copenagle, L., & Banker, G. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2625-06.2006 · Cited by 159
JNK signalling modulates intestinal homeostasis and tumourigenesis in mice
Sancho, R., Nateri, A. S., de Vinuesa, A. G., Aguilera, C. N., Nye, E. L., Spencer‐Dene, B., & Behrens, A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.153 · Cited by 161
Tumor Necrosis Factor-induced Long Myosin Light Chain Kinase Transcription Is Regulated by Differentiation-dependent Signaling Events
Graham, W. V., Wang, F., Clayburgh, D. R., Cheng, J. X., Yoon, B., Wang, Y., Lin, A., & Turner, J. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602164200 · Cited by 146
Self-citation
The Absence of NF-κB-Mediated Inhibition of c-Jun N-Terminal Kinase Activation Contributes to Tumor Necrosis Factor Alpha-Induced Apoptosis
Tang, F., Tang, G., Xiang, J., Dai, Q., Rosner, M. R., & Lin, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8571-8579.2002 · Cited by 145
Self-citation
The true face of JNK activation in apoptosis
Lin, A., & Dibling, B. C. (2002) · Aging Cell · doi:10.1046/j.1474-9728.2002.00014.x · Cited by 144
Self-citation
Regulation of Nur77 nuclear export by c-Jun N-terminal kinase and Akt
Han, Y.-H., Cao, X., Lin, B., Lin, F., Kolluri, S. K., Stebbins, J. L., Reed, J. C., Dawson, M. I., & Zhang, X.-K. (2006) · Oncogene · doi:10.1038/sj.onc.1209358 · Cited by 144
Regulation of human airway epithelial cell IL-8 expression by MAP kinases
Li, J., Kartha, S., Iasvovskaia, S., Tan, A., Bhat, R. K., Manaligod, J. M., Page, K., Brasier, A. R., & Hershenson, M. B. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00060.2002 · Cited by 144
HPK1 Is Activated by Lymphocyte Antigen Receptors and Negatively Regulates AP-1
Liou, J., Kiefer, F., Dang, A., Hashimoto, A., Cobb, M. H., Kurosaki, T., & Weiss, A. (2000) · Immunity · doi:10.1016/s1074-7613(00)80192-2 · Cited by 140
Selective Inactivation of c-Jun NH2-Terminal Kinase in Adipose Tissue Protects Against Diet-Induced Obesity and Improves Insulin Sensitivity in Both Liver and Skeletal Muscle in Mice
Zhang, X., Xu, A., Chung, S. K., Cresser, J., Sweeney, G., Wong, R. L. C., Lin, A., & Lam, K. S. L. (2011) · Diabetes · doi:10.2337/db10-0650 · Cited by 116
Self-citation
Distinct Roles for JNK and IKK Activation in Agouti-Related Peptide Neurons in the Development of Obesity and Insulin Resistance
Tsaousidou, E., Paeger, L., Belgardt, B., Pál, M., Wunderlich, C. M., Brönneke, H. S., Collienne, U., Hampel, B., Wunderlich, F. T., Schmidt‐Supprian, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.045 · Cited by 111
IRF5 and IRF5 Disease-Risk Variants Increase Glycolysis and Human M1 Macrophage Polarization by Regulating Proximal Signaling and Akt2 Activation
Hedl, M., Yan, J., & Abraham, C. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.060 · Cited by 107
The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization
Otto, I. M., Raabe, T., Rennefahrt, U. E. E., Peer Bork, B., Rapp, U. R., & Kerkhoff, E. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00388-2 · Cited by 101
NF-κB Is Required for UV-Induced JNK Activation via Induction of PKCδ
Liu, J., Yang, D., Minemoto, Y., Leitges, M., Rosner, M. R., & Lin, A. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.020 · Cited by 98
Self-citation
Involvement of c‐Jun N‐terminal kinase in amyloid precursor protein‐mediated neuronal cell death
Hashimoto, Y., Tsuji, O., Niikura, T., Yamagishi, Y., Ishizaka, M., Kawasumi, M., Chiba, T., Kanekura, K., Yamada, M., Tsukamoto, E., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01585.x · Cited by 99
Self-citation
Phosphorylation of DGCR8 Increases Its Intracellular Stability and Induces a Progrowth miRNA Profile
Herbert, K. M., Pimienta, G., DeGregorio, S. J., Alexandrov, A., & STEITZ, J. A. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.017 · Cited by 100
Transcriptional Regulation of EGR-1 by the Interleukin-1-JNK-MKK7-c-Jun Pathway
Hoffmann, E., Ashouri, J. F., Wolter, S., Doerrie, A., Dittrich‐Breiholz, O., Schneider, H., Wagner, E. F., Troppmair, J., Mackman, N., & Kracht, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800583200 · Cited by 97
A Novel c-Jun N-terminal Kinase (JNK)-binding Protein WDR62 Is Recruited to Stress Granules and Mediates a Nonclassical JNK Activation
Wasserman, T., Cohen‐Katsenelson, K., Daniliuc, S., Hasin, T., Choder, M., & Aronheim, A. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-06-0512 · Cited by 97
JNK: A Key Modulator of Intracellular Signaling
Vlahopoulos, S., & Zoumpourlis, V. C. (2004) · Biochemistry (Moscow) · doi:10.1023/b:biry.0000040215.02460.45 · Cited by 90
The Links between Transcription, β-catenin/JNK Signaling, and Carcinogenesis
Saadeddin, A., Babaei‐Jadidi, R., Spencer‐Dene, B., & Nateri, A. S. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0027 · Cited by 85
ATF1 Phosphorylation by the ERK MAPK Pathway Is Required for Epidermal Growth Factor-induced c-jun Expression
Gupta, P., & Prywes, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209799200 · Cited by 83
Active Mutants of the Human p38α Mitogen-activated Protein Kinase
Diskin, R., Askari, N., Capone, R. F., Engelberg, D., & Livnah, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404595200 · Cited by 82
Isolation of Hyperactive Mutants of the MAPK p38/Hog1 That Are Independent of MAPK Kinase Activation
Bell, M. I., Capone, R. F., Pashtan, I. M., Levitzki, A., & Engelberg, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101818200 · Cited by 82
Tauroursodeoxycholate inhibits human cholangiocarcinoma growth via Ca2+-, PKC-, and MAPK-dependent pathways
Alpini, G. D., Kanno, N., Phinizy, J. L., Glaser, S. S., Francis, H., Taffetani, S., & LeSage, G. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00270.2003 · Cited by 70
Mixed Lineage Kinase-3/JNK1 Axis Promotes Migration of Human Gastric Cancer Cells following Gastrin Stimulation
Mishra, P., Subramanian, S., Rangasamy, V., Sondarva, G. V., & Rana, B. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0387 · Cited by 71
Skeletal muscle-specific overproduction of constitutively activated c-Jun N-terminal kinase (JNK) induces insulin resistance in mice
Henstridge, D. C., Bruce, C. R., Pang, C. P., Lancaster, G. I., Allen, T. L., Estévez, E., Gardner, T., Weir, J. M., Meikle, P. J., Lam, K. S. L., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2652-8 · Cited by 67
Wiring the cell signaling circuitry by the NF-κB and JNK1 crosstalk and its applications in human diseases
Liu, J., & Lin, A. (2007) · Oncogene · doi:10.1038/sj.onc.1210417 · Cited by 67
Self-citation
Induction of Cytosolic Phospholipase A2 by Oncogenic Ras Is Mediated through the JNK and ERK Pathways in Rat Epithelial Cells
Putten, V. V., Refaat, Z. A., Dessev, C., Blaine, S. A., Wick, M. J., Butterfield, L., Han, S., Heasley, L. E., & Nemenoff, R. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003581200 · Cited by 68
p38α Antagonizes p38γ Activity through c-Jun-dependent Ubiquitin-proteasome Pathways in Regulating Ras Transformation and Stress Response
Qi, X.-M., Pohl, N. M., Loesch, M., Hou, S., Li, R., Qin, J., Cuenda, A., & Chen, G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703857200 · Cited by 65
The IL18RAP Region Disease Polymorphism Decreases IL-18RAP/IL-18R1/IL-1R1 Expression and Signaling through Innate Receptor–Initiated Pathways
Hedl, M., Zheng, S., & Abraham, C. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302727 · Cited by 61
The Mitogen-Activated Protein Kinase Phosphatase Vaccinia H1–Related Protein Inhibits Apoptosis in Prostate Cancer Cells and Is Overexpressed in Prostate Cancer
Arnoldussen, Y. J., Lorenzo, P. I., Pretorius, M. E., Wæhre, H., Risberg, B. Å., Mælandsmo, G. M., Danielsen, H. E., & Saatcioglu, F. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1224 · Cited by 57
Regulation of Two JunD Isoforms by Jun N-terminal Kinases
Yazgan, O., & Pfarr, C. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204552200 · Cited by 56
Amino-terminal-derived JNK Fragment Alters Expression and Activity of c-Jun, ATF2, and p53 and Increases H2O2-induced Cell Death
Buschmann, T., Yin, Z., Bhoumik, A., & Ronai, Z. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910045199 · Cited by 55
Combination of Two Activating Mutations in One HOG1 Gene Forms Hyperactive Enzymes That Induce Growth Arrest
Yaakov, G., Bell, M. I., Hohmann, S., & Engelberg, D. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.14.4826-4840.2003 · Cited by 55
Basal c-Jun NH2-terminal protein kinase activity is essential for survival and proliferation of T-cell acute lymphoblastic leukemia cells
Cui, J., Wang, Q., Wang, J., Lv, M., Zhu, N., Li, Y., Feng, J., Shen, B., & Zhang, J. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0408 · Cited by 54
Molecular Mechanisms for Neuronal Cell Death by Alzheimer’s Amyloid Precursor Protein-Relevant Insults
Kawasumi, M., Hashimoto, Y., Chiba, T., Kanekura, K., Yamagishi, Y., Ishizaka, M., Tajima, H., Niikura, T., & Nishimoto, I. (2002) · Neurosignals · doi:10.1159/000067424 · Cited by 53
Induction of Smooth Muscle α-Actin in Vascular Smooth Muscle Cells by Arginine Vasopressin Is Mediated by c-Jun Amino-terminal Kinases and p38 Mitogen-activated Protein Kinase
Garat, C., Putten, V. V., Refaat, Z. A., Dessev, C., Han, S., & Nemenoff, R. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003000200 · Cited by 52
Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases
Laughlin, J. D., Nwachukwu, J. C., Figuera-Losada, M., Cherry, L., Nettles, K. W., & LoGrasso, P. V. (2012) · Structure · doi:10.1016/j.str.2012.09.021 · Cited by 50
“While these mutations do not yield constitutive activity (Zheng et al., 1999), they induce a different conformer for the A-loop, allowing us to ask how changing the A-loop conformer impacts the catalytic and peptidebinding sites.”
Background
Hyperactive Variants of p38α Induce, whereas Hyperactive Variants of p38γ Suppress, Activating Protein 1-mediated Transcription
Askari, N., Diskin, R., Avitzour, M., Capone, R. F., Livnah, O., & Engelberg, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608012200 · Cited by 49
Differential Gene Regulation by Specific Gain-of-function JNK1 Proteins Expressed in Swiss 3T3 Fibroblasts
Han, S., Kim, S.-H., & Heasley, L. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204270200 · Cited by 48
Interleukin-1β Stimulation of c-Jun NH2-Terminal Kinase Activity in Insulin-Secreting Cells
Major, C. D., & Wolf, B. A. (2001) · Diabetes · doi:10.2337/diabetes.50.12.2721 · Cited by 47
Collaboration of JNKs and ERKs in Nerve Growth Factor Regulation of the Neurofilament Light Chain Promoter in PC12 Cells
Zentrich, E., Han, S., Pessoa-Brandão, L., Butterfield, L., & Heasley, L. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107824200 · Cited by 47
Jun Kinase Delays Caspase-9 Activation by Interaction with the Apoptosome
Tran, T., Andreka, P. G., Rodrigues, C. O., Webster, K. A., & Bishopric, N. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702210200 · Cited by 45
Osmotic Stress Regulates Mammalian Target of Rapamycin (mTOR) Complex 1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor Protein Phosphorylation
Kwak, D., Choi, S., Jeong, H., Jang, J., Lee, Y., Jeon, H., Lee, M. N., Noh, J., Cho, K., Yoo, J. S., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.326538 · Cited by 44
Analyzing JNK and p38 mitogen-activated protein kinase activity
Whitmarsh, A. J., & Davis, R. J. (2001) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(01)32212-7 · Cited by 45
Constitutive JNK Activation in NIH 3T3 Fibroblasts Induces a Partially Transformed Phenotype
Rennefahrt, U. E. E., Illert, B., Kerkhoff, E., Troppmair, J., & Rapp, U. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203010200 · Cited by 44
Effects of KGF on Alveolar Epithelial Cell Transdifferentiation Are Mediated by JNK Signaling
Qiao, R., Yan, W., Clavijo, C. A., Mehrian‐Shai, R., Zhong, Q., Kim, K., Ann, D. K., Crandall, E. D., & Borok, Z. (2007) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0172oc · Cited by 43
Alteration of JNK-1 Signaling in Skeletal Muscle Fails to Affect Glucose Homeostasis and Obesity-Associated Insulin Resistance in Mice
Pál, M., Wunderlich, C. M., Spohn, G., Brönneke, H. S., Schmidt‐Supprian, M., & Wunderlich, F. T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054247 · Cited by 42
Dynamic Positive Feedback Phosphorylation of Mixed Lineage Kinase 3 by JNK Reversibly Regulates Its Distribution to Triton-soluble Domains
Schachter, K. A., Du, Y., Lin, A., & Gallo, K. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603324200 · Cited by 43
Self-citation
Simvastatin induces NFκB/p65 down-regulation and JNK1/c-Jun/ATF-2 activation, leading to matrix metalloproteinase-9 (MMP-9) but not MMP-2 down-regulation in human leukemia cells
Chen, Y., & Chang, L. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.09.026 · Cited by 41
p38 MAPK regulates steroidogenesis through transcriptional repression of STAR gene
Zaidi, S. K., Shen, W., Bittner, S., Bittner, A., McLean, M. P., Han, J., Davis, R. J., Kraemer, F. B., & Azhar, S. (2014) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0287 · Cited by 42
Nod2-Induced Autocrine Interleukin-1 Alters Signaling by ERK and p38 to Differentially Regulate Secretion of Inflammatory Cytokines
Hedl, M., & Abraham, C. (2012) · Gastroenterology · doi:10.1053/j.gastro.2012.08.048 · Cited by 40
TAM Receptor–Dependent Regulation of SOCS3 and MAPKs Contributes to Proinflammatory Cytokine Downregulation following Chronic NOD2 Stimulation of Human Macrophages
Zheng, S., Hedl, M., & Abraham, C. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401933 · Cited by 41
Activation of c‐Jun NH2‐terminal kinase is required for gemcitabine's cytotoxic effect in human lung cancer H1299 cells
Teraishi, F., Zhang, L., Guo, W., Dong, F., Davis, J. J., Lin, A., & Fang, B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.10.064 · Cited by 38
Self-citation
Mutational analysis of dishevelled genes in zebrafish reveals distinct functions in embryonic patterning and gastrulation cell movements
Xing, Y.-Y., Cheng, X.-N., Li, Y.-L., Zhang, C., Saquet, A., Liu, Y., Shao, M., & Shi, D. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007551 · Cited by 37
c‐jun N‐terminal kinase hyperphosphorylates R406W tau at the PHF‐1 site during mitosis
Tatebayashi, Y., Planel, E., Chui, D., Sato, S., Miyasaka, T., Sahara, N., Murayama, M., Kikuchi, N., Yoshioka, K., Rivka, R., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-4362fje · Cited by 33
IDH1 Mutation Promotes Tumorigenesis by Inhibiting JNK Activation and Apoptosis Induced by Serum Starvation
Jiang, B., Zhang, J., Xia, J., Zhao, W., Wu, Y., Shi, M., Luo, L., Zhou, H., Chen, A., Ma, H., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.053 · Cited by 33
High-throughput cellular assays for regulated posttranslational modifications
Robers, M. B., Horton, R. A., Bercher, M. R., Vogel, K. W., & Machleidt, T. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.09.012 · Cited by 30
Antagonistic interaction between IGF and Wnt/JNK signaling in convergent extension in Xenopus embryo
Carron, C., Bourdelas, A., Li, H., Boucaut, J., & Shi, D. (2005) · Mechanisms of Development · doi:10.1016/j.mod.2005.06.007 · Cited by 28
JNK-deficiency enhanced oncolytic vaccinia virus replication and blocked activation of double-stranded RNA-dependent protein kinase
Hu, W., Hofstetter, W. L., Guo, W., Li, H., Pataer, A., Peng, H., Guo, Z. S., Bartlett, D. L., Lin, A., Swisher, S. G., et al. (2008) · Cancer Gene Therapy · doi:10.1038/cgt.2008.32 · Cited by 28
Self-citation
TNFSF15 Promotes Antimicrobial Pathways in Human Macrophages and These Are Modulated by TNFSF15 Disease-Risk Variants
Sun, R., Hedl, M., & Abraham, C. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.08.003 · Cited by 29
A TPL2 (MAP3K8) disease-risk polymorphism increases TPL2 expression thereby leading to increased pattern recognition receptor-initiated caspase-1 and caspase-8 activation, signalling and cytokine secretion
Hedl, M., & Abraham, C. (2015) · Gut · doi:10.1136/gutjnl-2014-308922 · Cited by 26
Regulation of the osterix (Osx, Sp7) promoter by osterix and its inhibition by parathyroid hormone
Barbuto, R., & Mitchell, J. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0251 · Cited by 26
CD28 Is Not Required for c-Jun N-Terminal Kinase Activation in T Cells
Rivas, F. V., O’Herrin, S. M., & Gajewski, T. F. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.6.3123 · Cited by 25
MKK4/SEK1 Is Negatively Regulated through a Feedback Loop Involving the E3 Ubiquitin Ligase Itch
Ahn, Y., & Kurie, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.044958 · Cited by 25
MAPK signaling and a mobile scaffold complex regulate AMPA receptor transport to modulate synaptic strength
Hoerndli, F. J., Brockie, P. J., Wang, R., Mellem, J. E., Kallarackal, A. J., Doser, R. L., Pierce, D. M., Madsen, D. M., & Maricq, A. V. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110577 · Cited by 22
MAP-quest: Could we produce constitutively active variants of MAP kinases?
Askari, N., Diskin, R., Avitzour, M., Yaakov, G., Livnah, O., & Engelberg, D. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.03.015 · Cited by 21
BAD Ser128 Is Not Phosphorylated by c-Jun NH2-Terminal Kinase for Promoting Apoptosis
Zhang, J., Liu, J., Yu, C., & Lin, A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0576 · Cited by 20
Self-citation
Defective anchoring of JNK1 in the cytoplasm by MKK7 in Jurkat cells is associated with resistance to Fas-mediated apoptosis
Wang, J., Tang, R., Lv, M., Wang, Q., Zhang, X., Guo, Y., Chang, H., Qiao, C., Xiao, H., Li, X., et al. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-06-0492 · Cited by 19
Activation of NF-κB by hepatitis B virus X protein through an IκB kinase-independent mechanism
Purcell, N. H., Yu, C., He, D., Xiang, J., Paran, N., DiDonato, J. A., Yamaoka, S., Shaul, Y., & Lin, A. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.280.4.g669 · Cited by 17
Self-citation
Antagonistic effect of flavonoids on NSC-741909-mediated antitumor activity via scavenging of reactive oxygen species
Guo, W., Wei, X., Wu, S., Wang, L., Peng, H., Wang, J., & Fang, B. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.08.057 · Cited by 16
Recruitment of Nuclear Factor Y to the Inverted CCAAT Element (ICE) by c-Jun and E1A Stimulates Basal Transcription of the Bone Sialoprotein Gene in Osteosarcoma Cells
Su, M., Bansal, A. K., Mantovani, R., & Sodek, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501609200 · Cited by 16
Phosphorylation of Bcl-associated death protein (Bad) by erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes to survival of erythropoietin-dependent cells
Deng, H., Zhang, J., Yoon, T., Song, D., Li, D.-D., & Lin, A. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.11.011 · Cited by 15
Self-citation
Loss of p38δ mitogen-activated protein kinase expression promotes oesophageal squamous cell carcinoma proliferation, migration and anchorage-independent growth
O'Callaghan, C., Fanning, L. J., Houston, A. M., & Barry, Ó. P. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1968 · Cited by 15
Stress-Activated Protein Kinase JNK Modulates Depression-like Behaviors in Mice
Zhou, X., Yi, W., Zhi, Y.-Q., Yu, J., Lu, D., Luo, Z.-S., Yuan, L., Chen, L.-Y., Xu, Z., & Xu, D. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03209-x · Cited by 14
Androgen via p21 Inhibits Tumor Necrosis Factor α-induced JNK Activation and Apoptosis
Tang, F., Kokontis, J. M., Lin, Y.-T., Liao, S., Lin, A., & Xiang, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.042994 · Cited by 15
Self-citation
Tumor induction by activated JNK occurs through deregulation of cellular growth
Rennefahrt, U. E. E., Illert, B., Greiner, A., Rapp, U. R., & Troppmair, J. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.05.015 · Cited by 12
Distinct roles for the α, β and γ1 isoforms of protein phosphatase 1 in the outside-in αIIbβ3 integrin signalling-dependent functions
Khatlani, T., Kailasam, L., Alrehani, N., Pradhan, S., & Vijayan, V. K. (2012) · Thrombosis and Haemostasis · doi:10.1160/th12-04-0237 · Cited by 11
ERK and JNK activation is essential for oncogenic transformation by v-Rel
Králová, J., Sheely, J. I., Liss, A. S., & Bose, H. R. (2010) · Oncogene · doi:10.1038/onc.2010.359 · Cited by 9
Effects of the JNK inhibitor anthra[1,9-cd]pyrazol-6(2H)-one (SP-600125) on soluble guanylyl cyclase α1 gene regulation and cGMP synthesis
Krumenacker, J. S., Kots, A. Y., & Murad, F. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00057.2005 · Cited by 9
Role of C-Jun N-Terminal Kinases on a Stressed Epithelium: Time for Testing Isoform Specificity
Shashikanth, N., Alaidi, O., Basa, L., Taank, S., Rao, R., & Seetharaman, J. (2025) · Biology · doi:10.3390/biology14060649 · Cited by 8
Isolation of intrinsically active mutants of MAP kinases via genetic screens in yeast
Engelberg, D., & Livnah, O. (2006) · Methods · doi:10.1016/j.ymeth.2006.06.014 · Cited by 8
The association of the JNK scaffold protein, WDR62, with the mixed lineage kinase 3, MLK3
Hadad, M., Aviram, S., Darlyuk‐Saadon, I., Cohen‐Katsenelson, K., Whitmarsh, A. J., & Aronheim, A. (2015) · MAP Kinase · doi:10.4081/mk.2015.5307 · Cited by 5
Towards the elucidation of the regulatory network guiding the insulin producing cells’ differentiation
Καπασά, Μ., Vlachakis, D., Kostadima, M. A., Sotiropoulou, G., & Κοσσίδα, Σ. (2012) · Genomics · doi:10.1016/j.ygeno.2012.07.002 · Cited by 4

Authors: Zheng, C., Xiang, J., Hunter, T., & Lin, A.
Affiliations: University of Alabama at Birmingham (US)
Salk Institute for Biological Studies (US)
Corresponding author: Lin, Anning
ORCID: Xiang, Jialing
Hunter, Tony
Lin, Anning
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-10
Volume: 274
Issue: 41
Pages: 28966-28971
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.41.28966
OpenAlex: W2022805818
Cited by: 110
References: 60
Citations by year: 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2020: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 3 · 2014: 4 · 2013: 4 · 2012: 7
FWCI: 2.62
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7677 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r29ca073740-02)
National Cancer Institute (CA 73740)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: c-Jun N-terminal kinase, JNK1, constitutive kinase activation, MAPK signaling, JNK phosphorylation, Rac1, Cdc42, MEKK1, nuclear localization
MeSH terms: Fluorescent Antibody Technique, Gene Expression Regulation, HeLa Cells, Humans, Nuclear Proteins, Phosphorylation, Protein Kinases, Recombinant Fusion Proteins, Transfection, Signal Transduction, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase 7

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

The JNKK2-JNK1 Fusion Protein Acts As a Constitutively Active c-Jun Kinase That Stimulates c-Jun Transcription Activity

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