Docking domains and substrate-specificity determination for MAP kinases
Open accessAbstract
Signalling specificity in eukaryotic cells is maintained by several mechanisms. One mechanism by which mitogen-activated protein (MAP) kinases ensure their specificity of action is by interacting with their substrates through docking domains. These docking domains recruit the kinases to the correct substrates and enhance their fidelity and efficiency of action. Additional specificity determinants in the substrates serve to enhance the specificity of substrate phosphorylation by MAP kinases further.
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D-motifs facilitate binding between specific MAPKs and their partner proteins in MAPK signaling networks.
“D-motifs play an important role in MAPK signaling networks by facilitating binding between specific MAPKs and their partner proteins (16, 19-21).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [20]
Many MAPK docking motifs have been characterized in transcription factors whose activity is controlled by MAPK phosphorylation.
“Many MAPK docking motifs have been previously characterized in transcription factors whose activity is controlled by MAPK phosphorylation (20).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [20]
PNT domains are docking modules that interact with complementary docking sites on kinases.
“Thus, the PNT domains are docking modules, interacting with complementary docking sites on the kinases (103, 104).”
From Genomic and biochemical insights into the specificity of ETS transcription factors (2011) · cites this paper as [104]
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- Authors
- Sharrocks, A. D., Yang, S.-H., & Galanis, A.
- Affiliations
- University of Manchester (GB)
- Corresponding author
- Sharrocks, Andrew D
- ORCID
- Sharrocks, Andrew D
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 25
- Issue
- 9
- Pages
- 448-453
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2155158959
- Cited by
- 442
- References
- 38
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 15 · 2023: 13 · 2022: 7 · 2021: 6 · 2020: 8 · 2019: 10 · 2018: 13 · 2017: 8 · 2016: 15 · 2015: 13 · 2014: 14 · 2013: 17 · 2012: 23
- FWCI
- 1.84
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Newcastle University ePrints (Newcastle Univesity)
- Funders
- Lister Institute of Preventive Medicine
- Biotechnology and Biological Sciences Research Council
- 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 › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- mitogen-activated protein kinase, docking domains, substrate specificity, substrate phosphorylation, kinase-substrate interactions, mitogen-activated protein kinase signalling
- MeSH terms
- Amino Acid Sequence, Animals, Molecular Sequence Data, Protein Binding, Substrate Specificity, Transcription Factors, Signal Transduction, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Evolution, Molecular, Protein Isoforms, MAP Kinase Signaling System
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