Docking interactions in protein kinase and phosphatase networks
Abstract
To achieve high biological specificity, protein kinases and phosphatases often recognize their targets through interactions that occur outside of the active site. Although the role of modular protein-protein interaction domains in kinase and phosphatase signaling has been well characterized, it is becoming clear that many kinases and phosphatases utilize docking interactions - recognition of a short peptide motif in target partners by a groove on the catalytic domain that is separate from the active site. Docking is particularly prevalent in serine/threonine kinases and phosphatases, and is a versatile organizational tool for building complex signaling networks; it confers a high degree of specificity and, in some cases, allosteric regulation.
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For protein kinases and phosphatases, the docking binding surface is separate from the active site.
“In this type of interaction, which is referred to as docking for protein kinases and phosphatases, the binding surface is separate from the active site (7).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [7]
Upstream MAP2K activators bind the same MAPK surface as downstream substrates, phosphatases, and scaffolds through independently evolved linear motifs.
“These upstream activators bind to the same surface on their cognate MAPK as downstream MAPK substrates, inactivating phosphatases and protein scaffolds by their independently evolved linear motifs (7).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [7]
MAPKs have promiscuous active sites, so additional protein interaction sites are critical for determining MAPK pathway wiring.
“Similarly to many signaling enzymes, MAPKs contain promiscuous active sites. Therefore, additional protein interaction sites are critical for determining the wiring of MAPK pathways.”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [7]
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References 50 · Cited by 188
- Authors
- Reményi, A., Good, M. C., & Lim, W. A.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Lim, Wendell A
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 16
- Issue
- 6
- Pages
- 676-685
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2033036465
- Cited by
- 188
- References
- 50
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 7 · 2023: 6 · 2022: 11 · 2021: 6 · 2020: 6 · 2019: 5 · 2018: 8 · 2017: 5 · 2016: 12 · 2015: 8 · 2014: 6 · 2013: 12 · 2012: 5
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- 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 › Protein Structure and Dynamics
- Keywords
- protein docking, protein kinases, protein phosphatase, serine/threonine kinase, phosphatase, allosteric regulation, kinase signaling networks, protein-protein interaction
- MeSH terms
- Allosteric Regulation, Binding Sites, Models, Biological, Models, Molecular, Phosphoprotein Phosphatases, Protein Conformation, Protein Kinases, Drug Design, Signal Transduction, Protein Structure, Tertiary, MAP Kinase Signaling System, Multiprotein Complexes
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