The Differential Regulation of p38α by the Neuronal Kinase Interaction Motif Protein Tyrosine Phosphatases, a Detailed Molecular Study
Open accessAbstract
The MAP kinase p38α is essential for neuronal signaling. To better understand the molecular regulation of p38α we used atomistic and molecular techniques to determine the structural basis of p38α regulation by the two neuronal tyrosine phosphatases, PTPSL/PTPBR7 (PTPRR) and STEP (PTPN5). We show that, despite the fact that PTPSL and STEP belong to the same family of regulatory proteins, they interact with p38α differently and their distinct molecular interactions explain their different catalytic activities. Although the interaction of PTPSL with p38α is similar to that of the previously described p38α:HePTP (PTPN7) complex, STEP binds and regulates p38α in an unexpected manner. Using NMR and small-angle X-ray scattering data, we generated a model of the p38α:STEP complex and define molecular differences between its resting and active states. Together, these results provide insights into molecular regulation of p38α by key regulatory proteins.
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Reverse NMR titration studies coupled with NMR-constrained docking using HADDOCK led to a model of the full p38:STEP complex.
“Reverse NMR titration studies, which required the completion of the sequence-specific backbone assignment of STEP, 63 coupled with NMR-constrained docking using HADDOCK led to a model of the full p38:STEP complex [Fig.4(B)].60”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
NMR studies of p38 with the KIM-containing family of PTPs have demonstrated that while the KIM peptides of these proteins bind p38 via quite similar mechanisms, they interact with p38 outside of the KIM binding groove very differently, explaining their different biological activities.
“Specifically, NMR studies of p38 with the KIM containing family of PTPs have unequivocally demonstrated that while the KIM peptides of these proteins bind p38 via quite similar mechanisms, they interact with p38 outside of the KIM binding groove very differently explaining their different biological activities.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
The STEP catalytic domain binds p38 at the MAPK-specific insert, near the p38 activation loop.
“This structure showed that the STEP catalytic domain binds p38 at the MAPK-specific insert, near the p38 activation loop”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
STEP binding to p38 leads to multiple additional perturbed residues on p38, not perturbed by HePTP or PTPSL, including D177/M179/V183/A190 (activation loop), L247/K248/S254/R256 (MAPK insert), and E328 (αI-αL16 loop).
“NMR experiments showed, unexpectedly, that STEP binding to p38 leads to multiple additional perturbed residues on p38 (these residues are not perturbed by HePTP or PTPSL), including D177/M179/V183/A190 (activation loop), L247/K248/S254/R256 (MAPK insert) and E328 (aI-aL16 loop).60”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
While the mode of KIM binding to p38 is largely conserved among the KIM-PTP family, with the KIMs from PTPSL/STEP and HePTP engaging residues within all four hydrophobic and both electrostatic pockets of the MAPK KIM binding groove, they perturb it differently, especially in the U_A and U_B hydrophobic pockets.
“First, while the mode of KIM binding to p38 is largely conserved among the KIM-PTP family, with the KIMs from PTPSL/STEP and HePTP engaged residues within all four hydrophobic both electrostatic pockets of the MAPK KIM binding groove, they perturb it differently, especially in the U A and U B hydrophobic pockets.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
Residue L108 from p38, which functions as a hinge connecting the p38 N- and C-terminal lobes, experiences CSPs with HePTP and PTPSL, but not STEP.
“Second, residue L108 from p38, which functions as a hinge connecting the p38 Nand C-terminal lobes, experiences CSPs with HePTP and PTPSL, but not STEP.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
A significant rotation of the STEP catalytic domain is necessary to properly position the active site of STEP for catalysis.
“a significant rotation of the STEP catalytic domain is necessary to properly position the active site of STEP for catalysis”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
There are key differences in the mechanism of binding of HePTP, STEP, and PTPSL with p38.
“These experiments showed that while there are similarities, there are also key differences in the mechanism of binding of HePTP, STEP, and PTPSL with p38.58,60”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
Despite the fact that the KIM sequences of PTPSL and STEP are identical, the proteins bind p38 very differently.
“Thus, despite of the fact that the KIM sequences of PTPSL and STEP are identical, the proteins bind p38 very differently.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
While the p38:HePTP and p38:PTPSL complexes are elongated in solution, the p38:STEP complex is compact.
“Fourth, while the p38:HePTP and p38:PTPSL complexes are elongated in solution, the p38:STEP complex is compact.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
The orientation of the STEP catalytic domain in the p38:STEP resting-state complex is not conducive to dephosphorylation of the tyrosine residue in the p38 phosphorylation loop.
“the orientation of the STEP catalytic domain in the p38:STEP resting-state complex is not conducive to dephosphorylation of the tyrosine residue in the p38 phosphorylation loop”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [60]
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“NMR experiments showed, unexpectedly, that STEP binding to p38 leads to multiple additional perturbed residues on p38 (these residues are not perturbed by HePTP or PTPSL), including D177/M179/V183/A190 (activation loop), L247/K248/S254/R256 (MAPK insert) and E328 (aIaL16 loop).(60) Thus, despite of the fact that the K…”
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- Authors
- Francis, D. M., Kumar, G. S., Koveal, D., Tortajada, A., Page, R., & Peti, W.
- Affiliations
- Brown University (US)
- Corresponding author
- Peti, Wolfgang
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 21
- Issue
- 9
- Pages
- 1612-1623
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC3769431
- OpenAlex
- W2050122396
- Cited by
- 21
- References
- 47
- Citations by year
- 2025: 1 · 2023: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2017: 2 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 3
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Energy
- American Cancer Society
- National Institutes of Health
- Office of Science
- National Institute of General Medical Sciences (T32GM008275, R01GM100910, T32GM007601)
- National Center for Research Resources (S10RR017269)
- Basic Energy Sciences
- Brookhaven National Laboratory
- 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, protein-protein interaction, neuronal signaling
- MeSH terms
- Humans, Models, Molecular, Protein Binding, Thermodynamics, X-Ray Diffraction, Catalytic Domain, Protein Structure, Quaternary, Mitogen-Activated Protein Kinase 14, Scattering, Small Angle, Protein Tyrosine Phosphatases, Non-Receptor, Receptor-Like Protein Tyrosine Phosphatases, Class 7, Protein Interaction Domains and Motifs
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