The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1
Open accessAbstract
Activation of the various mitogen-activated protein (MAP) kinase pathways converts many different extracellular stimuli into specific cellular responses by inducing the phosphorylation of particular groups of substrates. One important determinant for substrate specificity is likely to be the amino-acid sequence surrounding the phosphorylation site; however, these sites overlap significantly between different MAP kinase family members. The idea is now emerging that specific docking sites for protein kinases are involved in the efficient binding and phosphorylation of some substrates [1] [2] [3] [4]. The MAP kinase-activated protein (MAPKAP) kinase p90 rsk contains two kinase domains [5]: the amino-terminal domain (D1) is required for the phosphorylation of exogenous substrates whereas the carboxy-terminal domain (D2) is involved in autophosphorylation. Association between the extracellular signal-regulated kinase (Erk) MAP kinases and p90(rsk) family members has been detected in various cell types including Xenopus oocytes [6] [7] [8], where inactive p90(rsk) is bound to the inactive form of the Erk2- like MAP kinase p42(mpk1). Here, we identify a new MAP kinase docking site located at the carboxyl terminus of p90(rsk). This docking site was required for the efficient phosphorylation and activation of p90(rsk) in vitro and in vivo and was also both necessary and sufficient for the stable and specific association with p42(mpk1). The sequence of the docking site was conserved in other MAPKAP kinases, suggesting that it might represent a new class of interaction motif that facilitates efficient and specific signal transduction by MAP kinases.
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“MAPKAPKs form specific complexes with their activating enzyme through short (<20 amino acid) C-terminal docking motifs (25).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [25]
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“This region mediates binding to the MAPK docking groove located on ERK or p38 and this association is indispensable for MAPKAPK activation in cells (25).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [25]
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“MAPKAPKs are MAPK activated protein kinases that are comprised of a conserved calcium/calmodulin-dependent (CaMK)-type protein kinase domain and a C-terminal extension that enables activation by various MAPKs (ERK, p38 or both) (25).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [25]
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Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
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Palmer, A., Gavin, A., & Nebreda, A. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5037 · Cited by 330
Self-citationPulido, R., Zúñiga, Á., & Ullrich, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7337 · Cited by 320
Differential targeting of MAP kinases to the ETS‐domain transcription factor Elk‐1
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Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586
Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540
Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
Kölch, W. (2000) · Biochemical Journal · doi:10.1042/bj3510289 · Cited by 1,443
Metadata
- Authors
- Gavin, A.-C., & Nebreda, A. R.
- Affiliations
- European Molecular Biology Laboratory (DE)
- ORCID
- Gavin, Anne-Claude
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 1999-03
- Volume
- 9
- Issue
- 5
- Pages
- 281-286
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2059986458
- Cited by
- 158
- References
- 18
- Citations by year
- 2023: 3 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 4 · 2016: 2 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 2
- FWCI
- 6.09
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, other-oa)
- Funders
- Fonds De La Recherche Scientifique - FNRS
- 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
- p90RSK, protein phosphorylation, kinase activation, p42 MAP kinase, C-terminal domain, substrate specificity, MAPK signaling, protein-protein interaction motifs
- MeSH terms
- MAP-Kinase-Activated Kinase 2, Amino Acid Sequence, Animals, Binding Sites, Enzyme Activation, Humans, Molecular Sequence Data, Phosphorylation, Recombinant Fusion Proteins, Xenopus, Protein Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, Mitogen-Activated Protein Kinase 1, Ribosomal Protein S6 Kinases, 90-kDa, Intracellular Signaling Peptides and Proteins
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