Docking interactions in the mitogen-activated protein kinase cascades
Abstract
Regulation of cellular functions and responses utilizes a number of the signal transduction pathways. Each pathway should transduce signals with high efficiency and fidelity to avoid unnecessary crosstalks. The mitogen-activated protein kinase (MAPK) cascades regulate a wide variety of cellular functions, including cell proliferation, differentiation, and stress responses. MAPK is activated by MAPK kinase; phosphorylates various targets, including transcription factors and MAPK-activated protein kinases; and is inactivated by several phosphatases. Recent studies have provided a cue to understand the molecular mechanism underlying the signal transduction through the MAPK cascades. In the MAPK cascades, docking interactions, which are achieved through a site outside the catalytic domain of MAPKs, regulate the efficiency and specificity of the enzymatic reactions. The docking interaction is different from a transient enzyme-substrate interaction through the active center. It has been shown that activators, substrates, and inactivators of MAPKs utilize a common site on MAPKs in the docking interaction. Then, the docking interaction may regulate not only the efficiency and specificity of the cascades, but also the ordered and integrated signaling.
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MAPKs contain a docking groove that binds linear motifs in partner proteins.
“Mitogen activated protein kinases (MAPKs) have a docking groove that interacts with linear motifs in binding partners.”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [6]
MAPKs regulate diverse cellular processes and interact with proteins through linear binding motifs.
“Mitogen activated protein kinases (MAPKs) regulate diverse aspects of cellular life such as cell division, differentiation or apoptosis and interact with proteins through linear binding motifs (5-6).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [6]
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- Authors
- Tanoue, T., & Nishida, E.
- Affiliations
- Kyoto University (JP)
- Corresponding author
- Nishida, Eisuke
- ORCID
- Nishida, Eisuke
- Venue
- Pharmacology & Therapeutics
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 93
- Issue
- 2-3
- Pages
- 193-202
- ISSN
- 0163-7258 (ISSN-L)
- OpenAlex
- W1992023215
- Cited by
- 134
- References
- 57
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 8 · 2022: 7 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 1 · 2016: 7 · 2015: 4 · 2014: 8 · 2013: 5 · 2012: 5
- FWCI
- 0.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Pharmacology & Therapeutics (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 › Melanoma and MAPK Pathways
- Keywords
- mitogen-activated protein kinase, MAPK signaling, MAPK kinase, signal transduction, enzyme regulation, signaling specificity, signaling crosstalk, MAPK phosphorylation
- MeSH terms
- Animals, Humans, Membrane Proteins, Molecular Biology, Phosphorylation, Signal Transduction, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System
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