An essential role of the JIP1 scaffold protein for JNK activation in adipose tissue
Open accessAbstract
The c-Jun NH 2-terminal kinase (JNK) is activated during obesity. One consequence of obesity is that JNK phosphorylates the adapter protein insulin receptor substrate 1 (IRS-1) on Ser 307 and inhibits signaling by the insulin receptor. JNK can therefore cause peripheral insulin resistance during obesity and may contribute to the development of type 2 diabetes. Here we report that the JNK-interacting protein 1 (JIP1) scaffold protein, which binds components of the JNK signaling module, is essential for JNK activation in the adipose tissue of obese mice. These data identify JIP1 as a novel molecular target for therapeutic intervention in the development of obesity.
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JIP1 is a cytoplasmic scaffold that interacts with JNK-activating kinases and is needed for JNK activity in several settings, including obesity-induced insulin resistance.
“JIP1 is a cytoplasmic scaffold protein that interacts with the upstream activating kinases for JNK, and is required for activity in a number of different contexts, including regulation of obesity-induced insulin resistance (Jaeschke et al., 2004; Morel et al., 2010; Weston and Davis, 2007; Whitmarsh et al., 2001).”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Jaeschke et al., 2004
More physiological studies show that JIP1 is required for JNK activation and is inhibitory only when overexpressed.
“However, it is now clear from more physiologically relevant studies that JIP1 is required for activation of JNK (Jaeschke et al., 2004; Morel et al., 2010; Whitmarsh et al., 2001), and is only inhibitory when overexpressed.”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Jaeschke et al., 2004
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Yamauchi, T., Kamon, J., Waki, H., Terauchi, Y., Kubota, N., Hara, K., Mori, Y., Ide, T., Murakami, K., Tsuboyama-Kasaoka, N., et al. (2001) · Nature Medicine · doi:10.1038/90984 · Cited by 4,915 · see citing works
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works
A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359 · see citing works
The Continuing Epidemics of Obesity and Diabetes in the United States
Mokdad, A. H. (2001) · JAMA · doi:10.1001/jama.286.10.1195 · Cited by 2,730 · see citing works
The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
Berg, A. H., Combs, T. P., Du, X., Brownlee, M., & Scherer, P. E. (2001) · Nature Medicine · doi:10.1038/90992 · Cited by 2,526 · see citing works
Protection from obesity-induced insulin resistance in mice lacking TNF-α function
Uysal, K. T., Wiesbrock, S. M., Marino, M. W., & Hotamisligil, G. S. (1997) · Nature · doi:10.1038/39335 · Cited by 2,234 · see citing works
Role of Fatty Acids in the Pathogenesis of Insulin Resistance and NIDDM
Boden, G. (1997) · Diabetes · doi:10.2337/diab.46.1.3 · Cited by 1,728 · see citing works
Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487 · see citing works
Self-citationMichael, M. D., Kulkarni, R. N., Postic, C., Previs, S. F., Shulman, G. I., Magnuson, M. A., & Kahn, C. R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00015-8 · Cited by 1,296 · see citing works
Adiponectin and Metabolic Syndrome
Matsuzawa, Y., Funahashi, T., Kihara, S., & Shimomura, I. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000099786.99623.ef · Cited by 1,203 · see citing works
Aguirre, V., Werner, E. D., Giraud, J., Lee, Y. H., Shoelson, S. E., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m101521200 · Cited by 1,010 · see citing works
Regulation of MAP Kinase Signaling Modules by Scaffold Proteins in Mammals
Morrison, D. K., & Davis, R. J. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111401.091942 · Cited by 787 · see citing works
Self-citationA Cytoplasmic Inhibitor of the JNK Signal Transduction Pathway
Dickens, M., Rogers, J. S., Cavanagh, J., Raitano, A., Xia, Z., Halpern, J. R., Greenberg, M. E., Sawyers, C. L., & Davis, R. J. (1997) · Science · doi:10.1126/science.277.5326.693 · Cited by 675 · see citing works
Self-citationA Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation
Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J. (1998) · Science · doi:10.1126/science.281.5383.1671 · Cited by 652 · see citing works
Self-citationMatsuzawa, Y., Funahashi, T., & Nakamura, T. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07793.x · Cited by 601 · see citing works
Targeting JNK for therapeutic benefit: from junk to gold?
Manning, A. M., & Davis, R. J. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1132 · Cited by 585 · see citing works
Self-citationThe JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins
Yasuda, J., Whitmarsh, A. J., Cavanagh, J., Sharma, M., & Davis, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.7245 · Cited by 458 · see citing works
Self-citationc-Jun N-terminal Kinase (JNK) Mediates Feedback Inhibition of the Insulin Signaling Cascade
Lee, Y. H., Giraud, J., Davis, R. J., & White, M. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208359200 · Cited by 441 · see citing works
Self-citationRequirement of the JIP1 scaffold protein for stress-induced JNK activation
Whitmarsh, A. J., Kuan, C.-Y., Kennedy, N. J., Kelkar, N., Haydar, T. F., Mordes, J. P., Appel, M., Rossini, A. A., Jones, S. N., Flavell, R. A., et al. (2001) · Genes & Development · doi:10.1101/gad.922801 · Cited by 238 · see citing works
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Waeber, G., Delplanque, J., Bonny, C., Mooser, V., Steinmann, M., Widmann, C., Maillard, A. M., Judith Miklossy, A., Christian Dina, C., Hani, E. H., et al. (2000) · Nature Genetics · doi:10.1038/73523 · Cited by 182 · see citing works
JNK: a new therapeutic target for diabetes
Bennett, B. L. (2003) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(03)00068-7 · Cited by 151 · see citing works
IB1, a JIP-1-related Nuclear Protein Present in Insulin-secreting Cells
Bonny, C., NICOD, P. H., & Waeber, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.1843 · Cited by 139 · see citing works
Knockout models are useful tools to dissect the pathophysiology and genetics of insulin resistance
Mauvais‐Jarvis, F., Kulkarni, R., & Kahn, C. R. (2002) · Clinical Endocrinology · doi:10.1046/j.1365-2265.2002.01563.x · Cited by 82 · see citing works
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Thompson, N. A., Haefliger, J., Senn, A. P., Tawadros, T., Magara, F., Ledermann, B., NICOD, P. H., & Waeber, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100222200 · Cited by 56 · see citing works
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 · see citing works
Self-citationRepression of phospho‐JNK and infarct volume in ischemic brain of JIP1‐deficient mice
Im, J., Lee, K., Kim, M. H., Lee, S. H., Ha, H., Cho, I. J., Kim, D., Yu, M. S., Kim, J., Lee, J., et al. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10761 · Cited by 35 · see citing works
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Wu, W., Zhang, J., Zhao, C., Sun, Y., Pang, W., & Yang, G. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b00594 · Cited by 67 · see citing works
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“…scaffold protein that interacts with the upstream activating kinases for JNK, and is required for activity in a number of different contexts, including regulation of obesity-induced insulin resistance (Jaeschke et al., 2004; Morel et al., 2010; Weston and Davis, 2007; Whitmarsh et al., 2001).”
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Morel, C., Standen, C. L., Jung, D. Y., Gray, S., Ong, H., Flavell, R. A., Kim, J. K., & Davis, R. J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00585-10 · Cited by 30 · see citing works
Self-citationSrc Family Kinases Directly Regulate JIP1 Module Dynamics and Activation
Nihalani, D., Wong, H. N., Verma, R. K., & Holzman, L. B. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01479-06 · Cited by 30 · see citing works
Vaccinia Virus B1R Kinase Interacts with JIP1 and Modulates c-Jun-Dependent Signaling
Santos, C. R., Blanco, S., Sevilla, A., & Lazo, P. A. (2006) · Journal of Virology · doi:10.1128/jvi.00967-06 · Cited by 29 · see citing works
Human Protein Kinases and Obesity
Engin, A. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-48382-5_5 · Cited by 29 · see citing works
Phosphorylation of IRS1 at serine 307 and serine 312 in response to insulin in human adipocytes
Danielsson, A., Nyström, F. H., & Strålfors, P. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.075 · Cited by 26 · see citing works
Peptides as Signaling Inhibitors for Mammalian MAP Kinase Cascades
Gaestel, M., & Kracht, M. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209788682299 · Cited by 25 · see citing works
The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity
Xie, J., Onnockx, S., Vandenbroere, I., Degraef, C., Erneux, C., & Pirson, I. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.03.010 · Cited by 24 · see citing works
Intrinsic disorder in proteins associated with oxidative stress-induced JNK signaling
Gehi, B. R., Gadhave, K., Uversky, V. N., & Giri, R. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04230-4 · Cited by 23 · see citing works
Protein Kinases in Obesity, and the Kinase-Targeted Therapy
Engin, A. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-63657-8_7 · Cited by 25 · see citing works
Satoh, T., Abiru, N., Kobayashi, M., Zhou, H., Nakamura, K., Kuriya, G., Nakamura, H., Nagayama, Y., Kawasaki, E., Yamasaki, H., et al. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0576-2 · Cited by 23 · see citing works
Inflammation and Insulin Resistance: An Old Story with New Ideas
Kim, J. K. (2010) · Korean Diabetes Journal · doi:10.4093/kdj.2010.34.3.137 · Cited by 19 · see citing works
Ectopic overexpression of MCPIP1 impairs adipogenesis by modulating microRNAs
Łośko, M., Lichawska-Cieślar, A., Kulecka, M., Paziewska, A., Rumieńczyk, I., Mikuła, M., & Jura, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.09.010 · Cited by 18 · see citing works
Neacsu, O., Cleveland, K., Xu, H., Tchkonia, T., Kirkland, J. L., & Boney, C. M. (2013) · Obesity · doi:10.1002/oby.20329 · Cited by 18 · see citing works
Mingo-Sion, A. M., Ferguson, H. A., Koller, E., Reyland, M. E., & Berg, C. L. V. D. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-0669-0 · Cited by 17 · see citing works
Yu, W., Chen, C., Peng, Y., Li, Z., Gao, Y., Liang, S., Yuan, B., Kim, N., Jiang, H., & Zhang, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413630 · Cited by 15 · see citing works
Standen, C. L., Kennedy, N. J., Flavell, R. A., & Davis, R. J. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00155-09 · Cited by 15 · see citing works
Self-citationMitogen-activated protein kinase phosphatase-1: function and regulation in bone and related tissues
Broome, D. T., & Datta, N. S. (2016) · Connective Tissue Research · doi:10.3109/03008207.2015.1125480 · Cited by 14 · see citing works
Splice variant-specific stabilization of JNKs by IB1/JIP1
Yang, J.-Y., Moulin, N., Bemmelen, M. X. V., Dubuis, G., Tawadros, T., Haefliger, J., Waeber, G., & Widmann, C. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.07.001 · Cited by 12 · see citing works
Zhong, L., Luo, Y., Huang, C., & Liu, L. (2011) · Diabetes & Metabolism · doi:10.1016/j.diabet.2011.04.004 · Cited by 10 · see citing works
JIP1 Deficiency Protects Retinal Ganglion Cells From Apoptosis in a Rotenone-Induced Injury Model
Liu, W., Li, X., Chen, X., Zhang, J., Luo, L., Hu, Q., Zhou, J., Yan, J., Lin, S., & Ye, J. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00225 · Cited by 9 · see citing works
Liu, C.-P., Chau, P.-C., Chang, C.-T., An, L., Yeh, J., Chen, I., & Wu, B. (2018) · Molecules · doi:10.3390/molecules23102433 · Cited by 9 · see citing works
Evidence for tuning adipocytes ICER levels for obesity care
Brajkovic, S., Marenzoni, R., Favre, D., Guérardel, A., Salvi, R., Beeler, N., Froguel, P., Vollenweider, P., Waeber, G., & Abderrahmani, A. (2012) · Adipocyte · doi:10.4161/adip.20000 · Cited by 7 · see citing works
Jang, W. H., Jeong, Y. J., Choi, S. H., Urm, S.-H., & Seog, D. (2016) · Biomedical Reports · doi:10.3892/br.2016.818 · Cited by 6 · see citing works
Heng, C., Wang, Y., Jiang, H., Gu, H., Li, Z., Niu, M.-M., Zhang, M., & Li, J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117892 · Cited by 5 · see citing works
Inactivation of Minar2 in mice hyperactivates mTOR signaling and results in obesity
Lotfollahzadeh, S., Xia, C., Amraei, R., Hua, N., Kandror, K. V., Farmer, S. R., Wei, W., Costello, C. E., Chitalia, V. C., & Rahimi, N. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101744 · Cited by 4 · see citing works
Chew, C.-H., Ng, D.-L., Tie, S.-W., Ong, P.-C., Lim, W.-S., Muhammad, T. S. T., & Choo, Q.-C. (2011) · Electronic Journal of Biotechnology · doi:10.2225/vol14-issue3-fulltext-9 · Cited by 3 · see citing works
Kennedy, N. J., & Davis, R. J. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00164-9 · Cited by 3 · see citing works
Self-citationZaater, M. A., Kerdawy, A. M. E., Mahmoud, W. R., & Abou‐Seri, S. M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142141 · Cited by 2 · see citing works
Wong, H. N., Qi, N., Arias, E. B., Cho, K. W., Nihalani, D., Cartee, G. D., & Holzman, L. B. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102244 · Cited by 2 · see citing works
Protein Kinase Interactions with Regulatory and Effector Proteins
Defnet, A. E., Martinez, R., & Shapiro, P. (2020) · Springer eBooks · doi:10.1007/978-3-030-48283-1_4 · Cited by 2 · see citing works
Saeed, R., Mohammed, A. K., Saleh, S. E., Aboshanab, K. M., Aboulwafa, M., & Taneera, J. (2023) · Metabolites · doi:10.3390/metabo13020307 · Cited by 2 · see citing works
Impact of Proinflammatory Cytokines on Adipocyte Insulin Signaling
Tanti, J., Jager, J., & MARCHAND‐BRUSTEL, Y. L. (2012) · Springer eBooks · doi:10.1007/978-2-8178-0343-2_21 · Cited by 1 · see citing works
Hepatic MAP kinase signaling pathways in APAP-induced cell death
Win, S., Than, T. A., & Kaplowitz, N. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15877-3.00021-1 · Cited by 1 · see citing works
- Authors
- Jaeschke, A., Czech, M. P., & Davis, R. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-08-15
- Volume
- 18
- Issue
- 16
- Pages
- 1976-1980
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC514178
- OpenAlex
- W2156584134
- Cited by
- 121
- References
- 26
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 4 · 2023: 3 · 2022: 3 · 2021: 6 · 2020: 6 · 2019: 5 · 2018: 6 · 2017: 5 · 2016: 6 · 2015: 4 · 2014: 2 · 2013: 5 · 2012: 3
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- Topics
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- JIP1, JNK activation, c-Jun NH2-terminal kinase, adipose tissue, obesity, insulin resistance, IRS-1, type 2 diabetes, scaffold proteins
- MeSH terms
- Adipose Tissue, Animals, Diet, Enzyme Activation, Insulin Resistance, Mice, Inbred C57BL, Nuclear Proteins, Trans-Activators, Mitogen-Activated Protein Kinase Kinases, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase 4, Adaptor Proteins, Signal Transducing, Mice
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