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A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation
Abstract
The c-Jun NH 2 -terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by the exposure of cells to multiple forms of stress. A putative scaffold protein was identified that interacts with multiple components of the JNK signaling pathway, including the mixed-lineage group of MAP kinase kinase kinases (MLK), the MAP kinase kinase MKK7, and the MAP kinase JNK. This scaffold protein selectively enhanced JNK activation by the MLK signaling pathway. These data establish that a mammalian scaffold protein can mediate activation of a MAP kinase signaling pathway.
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In the citing paper
“The JNK-interacting protein (JIP) was originally identified as a putative scaffold that binds components of the JNK signaling pathway (Whitmarsh et al., 1998).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Whitmarsh et al., 1998
In the citing paper
“JNK-interacting protein-1 (JIP1) was identified as a scaffolding protein of the JNK module in yeast two-hybrid analysis, enhancing the correspondent signaling through the pathway (Whitmarsh et al , 1998).”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Whitmarsh et al , 1998
In the citing paper
“Three proteins were found, the c-jun NH2-terminal kinase (JNK)–interacting proteins (JIPs) JIP-1, JIP-2, and JIP-3, which are scaffolding proteins for the JNK signaling pathway.”
From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Whitmarsh et al. 1998
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Cites
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
Self-citationSignaling Through Scaffold, Anchoring, and Adaptor Proteins
Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256
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
Self-citationSignal transduction by the c-Jun N-terminal kinase (JNK) — from inflammation to development
Ip, Y. T., & Davis, R. J. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80143-9 · Cited by 1,538
Self-citationRaingeaud, J., Whitmarsh, A. J., Barrett, T., Dérijard, B., & Davis, R. J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1247 · Cited by 1,280
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
Self-citationBagrodia, S., Dérijard, B., Davis, R. J., & Cerione, R. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.27995 · Cited by 636
Self-citationOsmotic Activation of the HOG MAPK Pathway via Ste11p MAPKKK: Scaffold Role of Pbs2p MAPKK
Posas, F., & Saito, H. (1997) · Science · doi:10.1126/science.276.5319.1702 · Cited by 565
Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae
Chol, K.-Y., Satterberg, B., Lyons, D. M., & Elion, E. A. (1994) · Cell · doi:10.1016/0092-8674(94)90427-8 · Cited by 502
Signal Transduction by Tumor Necrosis Factor Mediated by JNK Protein Kinases
Sluss, H. K., Barrett, T., Dérijard, B., & Davis, R. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.8376 · Cited by 457
Self-citation
Research works printed but not linked: 3
- Hirai S., Izawa M., Osada S., Spyrou G., Ohno S., Oncogene 12, 641 (1996);
- Deacon K., Blank J. L., ibid. 272, 14489 (1997);
- Sluss H. K., Barrett T., Dérijard B., Davis R. J., Mol. Cell. Biol. 14, 8376 (1994);
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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
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Lin, Y., Mettling, C., & Chou, C. (2000) · Molecular Cell Biology Research Communications · doi:10.1006/mcbr.2001.0286 · Cited by 1
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Metadata
- Authors
- Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Davis, Roger J.
- Venue
- Science
- Published
- 1998-09-11
- Volume
- 281
- Issue
- 5383
- Pages
- 1671-1674
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1967218150
- Cited by
- 652
- References
- 25
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 5 · 2022: 8 · 2021: 3 · 2020: 4 · 2019: 8 · 2018: 7 · 2017: 11 · 2016: 8 · 2015: 7 · 2014: 10 · 2013: 17 · 2012: 10
- FWCI
- 25.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Research Explorer (The University of Manchester) (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 › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- scaffold proteins, c-Jun NH2-terminal kinase, JNK activation, MAPK signaling, mixed lineage kinase, MKK7, MAP kinase kinase kinase, stress signaling, protein-protein interaction
- MeSH terms
- Mitogen-Activated Protein Kinase Kinase Kinase 11, Animals, Carrier Proteins, Cell Line, Chlorocebus aethiops, Enzyme Activation, Interleukin-1, Molecular Sequence Data, Protein Kinases, Recombinant Fusion Proteins, Signal Transduction, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, COS Cells, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, MAP Kinase Kinase Kinases, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase 7
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