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Interaction of a Mitogen-Activated Protein Kinase Signaling Module with the Neuronal Protein JIP3
Open accessAbstract
The c-Jun NH(2)-terminal kinase (JNK) group of mitogen-activated protein kinases (MAPKs) is activated in response to the treatment of cells with inflammatory cytokines and by exposure to environmental stress. JNK activation is mediated by a protein kinase cascade composed of a MAPK kinase and a MAPK kinase kinase. Here we describe the molecular cloning of a putative molecular scaffold protein, JIP3, that binds the protein kinase components of a JNK signaling module and facilitates JNK activation in cultured cells. JIP3 is expressed in the brain and at lower levels in the heart and other tissues. Immunofluorescence analysis demonstrated that JIP3 was present in the cytoplasm and accumulated in the growth cones of developing neurites. JIP3 is a member of a novel class of putative MAPK scaffold proteins that may regulate signal transduction by the JNK pathway.
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“The JIPs display a highly polarized subcellular localization at the tips of neuronal cell processes and in extended projections from the surface of insulinoma cells (Meyer et al. 1999; Yasuda et al. 1999; Kelkar et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Kelkar et al. 2000
In the citing paper
“JIP-3 (also known as JSAP) can form oligomeric complexes with itself and JIP-2 but has no sequence relationship to JIP-1 or JIP-2 (Ito et al. 1999; Kelkar et al. 2000).”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Kelkar et al. 2000
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Keeping Neuronal Cargoes on the Right Track: New Insights into Regulators of Axonal Transport
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JSAP 1 and JLP are required for ARF 6 localization to the midbody in cytokinesis
Baljinnyam, T., Sato, T., Radnaa, E., Yamashita, K., & Yoshioka, K. (2014) · Genes to Cells · doi:10.1111/gtc.12170 · Cited by 11
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Kinase Suppressor of Ras Couples Ras to the ERK Cascade during T Cell Development
Laurent, M. N., Ramirez, D. M., & Alberola‐Ila, J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.2.986 · Cited by 11
Yasuoka, H., Ihn, H., Medsger, T. A., Hirakata, M., Kawakami, Y., Ikeda, Y., & Kuwana, M. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.12.6883 · Cited by 11
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“The JNK ⁄ stress-activated protein kinase-associated protein 1 (JSAP1) [also known as JNK-interacting protein 3 (JIP3) or Sunday Driver (Syd)] has been identified as a scaffold protein for mammalian JNK signaling modules (Ito et al. 1999, 2000; Bowman et al. 2000; Kelkar et al. 2000).”
BackgroundRegulation of N-cadherin-based cell–cell interaction by JSAP1 scaffold in PC12h cells
Bayarsaikhan, M., Takino, T., Davaakhuu, G., Sato, H., Ito, T., & Yoshioka, K. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.029 · Cited by 10
“Because JSAP1 has been identified as a scaffold protein for JNK signaling [7,8], we asked whether the depletion of JSAP1 affects the activation of JNK during NGF-induced signaling in PC12h cells.”
BackgroundKoon, Y. L., Koh, C.-G., & Chiam, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092437 · Cited by 9
“It accumulates in the growth cones at the tips of extended neurites [31–33] as well as within cell surface projections of cultured cells [30].”
BackgroundZareifard, A., Beaudry, F., & Ndiaye, K. (2023) · BMC Molecular and Cell Biology · doi:10.1186/s12860-023-00482-5 · Cited by 10
“MAPK8IP3 has been reported as a scaffold protein within the JNK signaling cascade [62].”
BackgroundMutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity
Huang, J., Tu, Z., & Lee, F. S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00387-5 · Cited by 9
Chen, B., Ma, X., Geng, Z., Huang, S., Zhai, L., Guo, Y., & Chen, Z. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13226 · Cited by 9
“2006), and was originally identified for its role in organizing JNK signaling cascades by acting as a scaffold protein (Ito et al. 1999; Kelkar et al. 2000).”
BackgroundInfluentialYang, H., Wang, Q., Li, Q., He, L., & Yu, A.-Q. (2016) · Journal of Crustacean Biology · doi:10.1163/1937240x-00002468 · Cited by 8
“All JIP family members have been shown to contain a conserved region (JBD: JNK binding domain), which can bind JNK in mammals (Kelkar et al., 2000; Engstrom et al., 2010).”
BackgroundNam, Y., Cheon, H., Choi, Y. K., Kim, S.-Y., Shin, E., Kim, E., & Kim, H. K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.05.047 · Cited by 8
“protein to tether cargo to kinesin motor proteins [34].”
BackgroundCytoplasmic Tail Adaptors of Alzheimer's Amyloid-β Protein Precursor
Kawasumi, M., Matsuda, S., Matsuoka, M., & Nishimoto, I. (2004) · Molecular Neurobiology · doi:10.1385/mn:30:2:185 · Cited by 9
JSAP1 Interacts with Kinesin Light Chain 1 through Conserved Binding Segments
Kim, S., Lee, C.-H., Park, H.-Y., Yea, S.-S., Jang, W.-H., Lee, S.-K., Park, Y.-H., Cha, O.-S., Moon, I.-S., & Seog, D. (2007) · Journal of Life Science · doi:10.5352/jls.2007.17.7.889 · Cited by 8
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The scaffold protein JLP plays a key role in regulating ultraviolet B ‐induced apoptosis in mice
Radnaa, E., Sato, T., Wakasugi, M., Tuvshintugs, B., Miyata, H., Sakurai, T., Matsunaga, T., & Yoshioka, K. (2014) · Genes to Cells · doi:10.1111/gtc.12135 · Cited by 7
“JNK/stress-activated protein kinase-associated protein 1 (JSAP1, also known as JIP3 or Sunday Driver), which is highly homologous with JLP in its sequence and domain structure, has been identified as a scaffold protein for JNK signaling pathways (Ito et al. 1999; Kelkar et al. 2000).”
BackgroundCaswell, P. T., & Dickens, M. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3222-7 · Cited by 7
“This distribution was highly consistent with the distribution of JIP family proteins seen previously in many neuronal cell types [12, 19, 21, 23, 29, 41].”
BackgroundResultBorsello, T., Centeno, C., Riederer, I. M., Haefliger, J., & Riederer, B. M. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21435 · Cited by 7
“, 1998; Mooney and Whitmarsh, 2004), the MAP kinase kinase 7 (Yasuda et al., 1999; Kelkar et al., 2000; Whitmarsh et al., 2001; Mooney and Whitmarsh, 2004), and the MAPK phosphatase-7 (Willoughby et al.”
BackgroundSelective expression of the scaffold protein JSAP1 in spermatogonia and spermatocytes
Bayarsaikhan, M., Shiratsuchi, A., Davaakhuu, G., Nakanishi, Y., & Yoshioka, K. (2006) · Reproduction · doi:10.1530/rep.1.00939 · Cited by 7
“Since JSAP1 is expressed in the adult testis (Ito et al. 1999, Kelkar et al. 2000), it is speculated that JNK MAPK signaling pathways are involved in the regulation of gene expression during spermatogenesis.”
BackgroundA toxic gain-of-function variant in MAPK8IP3 provides insights into JIP3 cellular roles
Zhang, W., Mittal, S., Thomas, R., Foroughishafiei, A., Bastos, R. N., Chung, W. K., Skourti-Stathaki, K., & Crooke, S. T. (2025) · JCI Insight · doi:10.1172/jci.insight.187199 · Cited by 6
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“Introduction JIP3 and JIP4 (JNK-interacting proteins 3 and 4) were first identified as scaffold proteins for JNK and p38 mitogenactivated protein kinase (MAPK) signalling modules (Ito et al., 1999; Kelkar et al., 2000; Lee et al., 2002).”
BackgroundMLK 3 as a regulator of disease progression in Non‐alcoholic steatohepatitis
Jiang, J. X., & Torok, N. J. (2014) · Liver International · doi:10.1111/liv.12556 · Cited by 6
Critical role of JSAP1 and JLP in axonal transport in the cerebellar Purkinje cells of mice
Sato, T., Ishikawa, M., Yoshihara, T., Nakazato, R., Higashida, H., Asano, M., & Yoshioka, K. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.08.024 · Cited by 6
“JSAP1 and JLP were first identified as scaffolding proteins for mammalian JNK and p38 MAPK signaling modules [4,5,7,8].”
BackgroundCharacterization of signalling pathways in cardiac hypertrophic response
Koivisto, E. (2011) · Cited by 6
Koinuma, S., Miyaji, M., Akiyama, S., Ito, Y., Takemura, H., Wada, N., Igarashi, M., & Nakamura, T. (2025) · Journal of Cell Science · doi:10.1242/jcs.263636 · Cited by 5
Kinesin transport: driving kinesin in the neuron
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“c-Jun NH2-terminal kinase (JNK)-interacting protein 3 (JIP3) is a member of the JNK-binding protein family and, as a scaffold prote in for the JNK signaling pathway, facilitates JNK activation [10, 11].”
BackgroundJIP3 knockout protects mice against high fat diet-induced liver injury.
Ma, X.-J., Xing, H.-Z., Ren, G.-F., Rao, X.-J., & Li, Z.-Z. (2018) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2018.01.178 · Cited by 4
JSAP1 is required for the cell adhesion and spreading of mouse embryonic fibroblasts
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High-Throughput Multiomics Profiling of Model Systems Using the AVITI24 PlatformPreprint
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“For instance, phosphorylation of heat shock protein 27 (HSP27) enhances cell survival by stabilizing the cytoskeleton and inhibiting caspase activation, cooperating with anti-apoptotic BCL-2 family proteins to block apoptosis [23,24,25,26].”
Syd/JIP3 controls tissue size by regulating Diap1 protein turnover downstream of Yorkie/YAP
Ahmad, V., Vadla, G. P., & Chabu, C. Y. (2020) · Developmental Biology · doi:10.1016/j.ydbio.2020.09.017 · Cited by 4
The evolution of JNK inhibition: A review on modern targeting strategies
Li, J., Cao, L., Yang, Y., Gao, Y., Li, B., Shao, N., Ran, Z., & Luo, L. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.118787 · Cited by 3
Gunarta, I. K., Yuliana, D., Erdenebaatar, P., Kishi, Y., Boldbaatar, J., Suzuki, R., Odongoo, R., Davaakhuu, G., Hohjoh, H., & Yoshioka, K. (2021) · Drug Discoveries & Therapeutics · doi:10.5582/ddt.2021.01021 · Cited by 3
“JSAP1 has been identified as a scaffold protein for the JNK MAPK signaling pathway (7,8), as well as an adaptor for kinesin-1 and dynein motor proteins (1113).”
BackgroundSignal Transduction by the Ras–MAP Kinase Pathway in Prostate Cancer Progression
Gioeli, D. G., Kraus, S. R., & Weber, M. J. (2008) · Humana Press eBooks · doi:10.1007/978-1-60327-079-3_11 · Cited by 3
Mitogen-Activated Protein Kinase Cascades as Therapeutic Targets in Cancer
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“JIP1 and JIP2 binds to JNK, MKK7, and members of the mixed-lineage group of MAPKKK (Kelkar et al. 2000; Weston and Davis, 2002).”
BackgroundKennedy, N. J., & Davis, R. J. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00164-9 · Cited by 3
JNK‐interacting protein 4 is a central molecule for lysosomal retrograde trafficking
Sasazawa, Y., Hattori, N., & Saiki, S. (2023) · BioEssays · doi:10.1002/bies.202300052 · Cited by 2
Blocking Stress Signaling Pathways with Cell Permeable Peptides
Bonny, C. (2006) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-34817-9_12 · Cited by 2
Examining signaling specificity to transcription factors
Whitmarsh, A. J. (2002) · Methods · doi:10.1016/s1046-2023(02)00025-7 · Cited by 2
UNC-16/JIP3 inhibits the function of the regeneration promoting isoform of DLK-1Preprint
Kulkarni, S., Sabharwal, V., Sheoran, S., Basu, A., Matsumoto, K., Hisamoto, N., Ghosh-Roy, A., & Koushika, S. (2018) · bioRxiv · doi:10.1101/484683 · Cited by 1
“JIP3, the mammalian orthologue of UNC-16, is known to form a complex with DLK (Holland et al., 2016; Kelkar et al., 2000).”
BackgroundInfluentialSuzuki, R., Kanemaki, M. T., Suzuki, T., & Yoshioka, K. (2023) · Genes to Cells · doi:10.1111/gtc.13083 · Cited by 1
“JLP and its paralog JNK/stress-activated protein kinase-associated protein 1 (JSAP1) (Ito et al., 1999), also known as JIP3 (Kelkar et al., 2000), share similar domain structures, including JNK/p38 MAPK-binding domain (MBD) and kinesin-1 heavy chain (KHC)- binding domains (KBD) (Ito et al., 2000; Sun et al., 2011), su…”
BackgroundRegulatory role of N6-Methyladenosine on skeletal muscle development in Hu sheep
Jiang, J., Guo, L., Huang, X., Zheng, K., He, S., & Shan, H. (2024) · Frontiers in Genetics · doi:10.3389/fgene.2024.1449144 · Cited by 1
Biological Roles of MAP Kinases
De, S. K. (2024) · Springer eBooks · doi:10.1007/978-3-031-75682-5_2 · Cited by 1
Regulation of the JNK signaling pathway by dual leucine zipper kinase DLK
Ma, X., & Xue, L. (2010) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2010.00785 · Cited by 1
“DLK可通过支架蛋白JIP(JNK-interacting protein )分别与MKK7及JNK发生作用,从 而激活JNK信号传导通路([19])。JIP的作用主要体现在两个方面:1)通过对不同组分的募集造 成信号传导的特异性;2)通过形成稳定的复合物为MAPKKK到MAPK的信号传递提供空间 基础。实验表明,JIP-1可增强DLK诱导的JNK磷酸化,对JIP-1中的JNK结合位点进行突变后, DLK对JNK的激活能力受到抑制([20]),说明JIP对DLK诱导的JNK活化有着重要作用。进一步 的研究 揭示了DLK、JIP和JNK之间的相互作用及调控机制(图1)。正常情况下,JNK 级联反应中各激酶的活性维持在较低水平,JIP…”
BackgroundWITHDRAWN: JIP3 deficiency protects mice from high fat diet-induced liver injury.
Rao, X.-J., Wu, Y.-M., Wang, Y., & Shi, S. (2017) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2017.09.109 · Cited by 1
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Mechanisms of Hormone Signaling in Plants Under Abioticand Biotic Stresses
Panigrahi, J., & Rout, G. R. (2017) · doi:10.1002/9781118889022.ch35 · Cited by 1
Impairment of cardiomyogenesis in embryonic stem cells lacking scaffold protein JSAP1
Sato, T., Hidaka, K., Iwanaga, A., Ito, M., Asano, M., Nakabeppu, Y., Morisaki, T., & Yoshioka, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.10.052
Anti‐Inflammatory/Analgesics: An In‐Depth Look at p 38 MAP Kinases
Brown, K. L. (2011) · Wiley eBooks · doi:10.1002/9780470571224.pse446
The role of JNK2 and JNK1 in breast cancer mediated invasion and metastasis
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Mitogen-Activated Protein Kinases and Their Scaffolding Proteins
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INTEGRACIÓN DE LA FUNCIÓN DE VRK2 EN LAS RUTAS DE SEÑALIZACIÓN DE JNK Y P53.
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The β Subunit of Heterotrimeric G Protein Interacts Directly with Kinesin Heavy Chains, Kinesin-I
Seog, D. (2010) · Journal of Life Science · doi:10.5352/jls.2010.20.8.1166
“Kinesin-I binding proteins fall into six classes: mRNP transport, pathogen transport, slow axonal transport and movement of cytoskeleton subunits, transport of membrane-bound organelles, transport of signaling molecules to specific locations within the cell, and proteins that regulate kinesin-I activity [2,6,10,15,18,…”
BackgroundTherapeutic Implications of Ceramide-Regulated Signaling Cascades
KESTER, M. A., Yun, J. K., Stover, T., & Sandirasegarane, L. (2002) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-9272-7_16
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Zahayko, A. L., Krasilnikova, O. A., & Kravchenko, A. B. (2017) · Medical and Clinical Chemistry · doi:10.11603/mcch.2410-681x.2016.v0.i4.7289
Computational modelling of protein-protein and cell-cell interaction across multiple scales
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Vilela, F., Chenon, M., Campanacci, V., Alik, A., Velours, C., Andréani, J., Llinas, P., & Ménétrey, J. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5784569
A Syd and RUFY dynein adaptor complex mediates axonal circulation of dense core vesicles
Lund, V. K., Chirco, A., Caliari, M., Larsen, A. H., Tang, K. T., Gether, U., Madsen, K. L., Wierer, M., & Kjaerulff, O. (2026) · Journal of Cell Biology · doi:10.1083/jcb.202507071
“Besides the vesicular motor adaptor role, Syd/JIP3/4 proteins function as important scaffolds and transport adaptors for the JNK MAP kinase (Byrd et al., 2001; Ito et al., 1999; Kelkar et al., 2000).”
Role of ARF6 in breast cancer cell invasion
Marchesin, V. (2014) · theses.fr (ABES) · doi:10.70675/27f4caf2z487bz4570z9ceczcd69bf1d3ac9
“JIP3 is predominantly expressed in the brain both at the mRNA and protein levels as demonstrated by Northern and Western blot analysis, with lower levels in the heart and other tissues (Kelkar et al., 2000).”
InfluentialCaractérisation moléculaire et immunité des cancers du sein triple-négatifs
Bonsang‐Kitzis, H. (2018) · theses.fr (ABES) · doi:10.70675/285c912cz8251z4099z9cf7ze121cd7350d0
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“As a scaffold protein, MAPK8IP3/JIP3 interacts with specific components of the JNK pathway, regulating the efficiency and specificity of signal transduction [3,4].”
Vilela, F., Chenon, M., Campanacci, V., Alik, A., Velours, C., Andreani, J., Llinas, P., & Ménétrey, J. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113355 · Cited by 2
Ebrahimi, A., Chi, S., Yang, J., Lee, P. Y., Colling, P. K., Mendenhall, H., Wang, Z., Giusti, C., Foster, L. J., Hendrix, D. A., et al. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6c00109
Mantica, F., Torres-Méndez, A., Zapata-Bodalo, I., Iñiguez, L., Márquez, Y., Morin, V., Roignant, J., & Irimia, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.05.749416
Neural-specific ablation of the scaffold protein JSAP1 in mice causes neonatal death
Iwanaga, A., Sato, T., Sugihara, K., Hirao, A., Takakura, N., Okamoto, H., Asano, M., & Yoshioka, K. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.09.057
Metadata
- Authors
- Kelkar, N., Gupta, S., Dickens, M., & Davis, R. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Davis, Roger J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2000-02-01
- Volume
- 20
- Issue
- 3
- Pages
- 1030-1043
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC85220
- OpenAlex
- W2147103035
- Cited by
- 281
- References
- 71
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 2 · 2023: 4 · 2022: 7 · 2021: 5 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 10 · 2016: 7 · 2015: 9 · 2014: 8 · 2013: 7 · 2012: 6
- FWCI
- 8.62
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (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 Cancer Institute
- 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
- JIP3, JNK, c-Jun NH2-terminal kinase, MAPK signaling, MAPK kinase, MAPK kinase kinase, growth cones, neurite development, signal transduction regulation, brain expression
- MeSH terms
- Aging, Amino Acid Sequence, Animals, Brain, Cells, Cultured, Cloning, Molecular, Enzyme Activation, Female, Embryonic and Fetal Development, Male, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Recombinant Proteins, Signal Transduction, Gene Library, Sequence Alignment, Sequence Homology, Amino Acid, Gene Expression Regulation, Developmental, Protein Isoforms, Mitogen-Activated Protein Kinases, MAP Kinase Kinase Kinases, JNK Mitogen-Activated Protein Kinases, Adaptor Proteins, Signal Transducing, Mice
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