Structural Basis for the Regulation of the Mitogen-activated Protein (MAP) Kinase p38α by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution
Open accessAbstract
Mitogen-activated protein kinases (MAPKs) fulfill essential biological functions and are key pharmaceutical targets. Regulation of MAPKs is achieved via a plethora of regulatory proteins including activating MAPKKs and an abundance of deactivating phosphatases. Although all regulatory proteins use an identical interaction site on MAPKs, the common docking and hydrophobic pocket, they use distinct kinase interaction motif (KIM or D-motif) sequences that are present in linear, peptide-like, or well folded protein domains. It has been recently shown that a KIM-containing MAPK-specific dual specificity phosphatase DUSP10 uses a unique binding mode to interact with p38α. Here we describe the interaction of the MAPK binding domain of DUSP16 with p38α and show that despite belonging to the same dual specificity phosphatase (DUSP) family, its interaction mode differs from that of DUSP10. Indeed, the DUSP16 MAPK binding domain uses an additional helix, α-helix 4, to further engage p38α. This leads to an additional interaction surface on p38α. Together, these structural and energetic differences in p38α engagement highlight the fine-tuning necessary to achieve MAPK specificity and regulation among multiple regulatory proteins. Background: Dual specificity phosphatases play a crucial role in MAP kinase regulation. Results: DUSP16 (MKP7) and p38α interact in a unique manner that is different from other DUSPs. Conclusion: DUSP16 binds p38α via an extended binding surface that includes helix α4. Significance: This study shows that DUSPs interact differently with p38α and lays the structural basis for their differential regulation of MAPKs.
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In DUSP10/MKP5 and DUSP16/MKP7, binding of additional structural elements of DUSP16/MKP7 leads to an extended interaction surface and stronger binding.
“Furthermore, in the case of the MAPK-binding domains of DUSP10/ MKP5 and DUSP16/MKP7, which share a core interaction motif, binding of additional structural elements of DUSP16/MKP7 lead to an extended interaction surface and thus stronger binding.57”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [57]
The discrimination factor of DUSP16/MKP7 for p38 versus ERK is only 0.7.
“Indeed, we have observed the same behavior of KIM peptides/proteins using ITC; i.e., the discrimination factor of DUSP16/MKP7 (a p38/ JNK specific DUSP) for p38 versus ERK is only 0.7.57,58”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [57]
The MKBD of DUSP10/MKP5 and DUSP16/MKP7 are highly similar.
“The MKBD of DUSP10/MKP5 and DUSP16/MKP7 are highly similar, 35,57”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [57]
The interaction between the DUSP16/MKP7 MKBD with p38 also binds in a similar mostly C-to-N direction.
“we showed that while the interaction between the DUSP16/MKP7 MKBD with p38 also binds in a similar mostly C-to-N direction”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [57]
The DUSP16/MKP7 MKBD interaction with p38 is different from that of DUSP6 and DUSP10/MKP5, as it includes not only helix α2 and α3 (largely identical to the interaction of DUSP10/MKP5 MKBD) but also helix α4.
“it is also different from that of DUSP6 and DUSP10/ MKP5, as it includes not only helix a2 and a3 (largely identical to the interaction of DUSP10/ MKP5 MKBD) but also helix a4 [Figs.2(C), 4(B)].57”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [57]
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Self-citationGong, J., Li, C., Han, Q., Ma, S., He, J., Zhang, H., Rawdkuen, S., Hou, D., & Wu, S. (2026) · Research Square · doi:10.21203/rs.3.rs-10134917/v1
- Authors
- Kumar, G. S., Zettl, H., Page, R., & Peti, W.
- Affiliations
- Brown University (US)
- Corresponding author
- Peti, Wolfgang
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 288
- Issue
- 39
- Pages
- 28347-28356
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3784751
- OpenAlex
- W2093754311
- Cited by
- 12
- References
- 45
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 1
- FWCI
- 0.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM100910, R01GM098482)
- National Center for Research Resources (S10RR017269)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- 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 Structure and Dynamics
- Keywords
- p38α MAP kinase, DUSP16, dual-specificity phosphatase, protein-protein interaction, DUSP10
- MeSH terms
- Binding Sites, Calorimetry, Humans, Magnetic Resonance Spectroscopy, Protein Binding, Signal Transduction, Gene Expression Regulation, Enzymologic, Protein Structure, Tertiary, p38 Mitogen-Activated Protein Kinases, Dual-Specificity Phosphatases, Mitogen-Activated Protein Kinase Phosphatases
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