Quantifying ERK2–protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains
Abstract
While mitogen-activated protein kinase signaling pathways constitute highly regulated networks of protein-protein interactions, little quantitative information for these interactions is available. Here we highlight recent fluorescence anisotropy binding studies that focus on the interactions of ERK1 and ERK2 with PEA-15 (antiapoptotic phosphoprotein enriched in astrocytes-15 kDa), a small protein that sequesters ERK2 in the cytoplasm. The regulation of ERK2 by PEA-15 is appraised in the light of a simple equilibrium-binding model for reversible ERK2 nucleoplasmic-cytoplasmic shuttling, which elaborates on the theory of Burack and Shaw (J. Biol. Chem. 280, 3832-3837; 2005). Also highlighted is the recent observation that the peptide N-QKGKPRDLELPLSPSL-C, derived from the docking site for ERK/JNK and LEL (DEJL) in Elk-1, displaces PEA-15 from ERK2. It is proposed that the C-terminus of PEA-15 ((121)LXLXXXXKK(129)) is a reverse DEJL domain [which has a general consensus of R/K-phi(A)-X(3/4)-phi(B), where phi(A) and phi(B) are hydrophobic residues (Leu, Ile, or Val)], which mediates one arm of a bidentate PEA-15 interaction with ERK2. The notion that PEA-15 is a potent inhibitor of many ERK2-mediated phosphorylations, by virtue of its ability to block ERK2-DEJL domain interactions, is proposed.
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PEA-15 binds the ERK2 KIM binding groove in the non-canonical C-to-N direction.
“Similarly, previous studies showed that PEA-15 binds the ERK2 KIM binding groove in the non-canonical C->N direction [Fig.2(B)].75”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [75]
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Self-citationRegulation and inhibition of MAP kinases
Kaoud, T. S. (2012) · Texas ScholarWorks (Texas Digital Library)
- Authors
- Callaway, K., Rainey, M. A., & Dalby, K. N.
- Affiliations
- The University of Texas at Austin (US)
- Corresponding author
- Dalby, Kevin N.
- ORCID
- Dalby, Kevin N.
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2005-12
- Volume
- 1754
- Issue
- 1-2
- Pages
- 316-323
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2078834086
- Cited by
- 26
- References
- 65
- Citations by year
- 2023: 2 · 2022: 1 · 2020: 2 · 2019: 3 · 2013: 4 · 2012: 2
- FWCI
- 0.16
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM059802, GM59802)
- National Institute of Environmental Health Sciences (ES 07247, #ES07784, P30ES007784, T32ES007247)
- National Center for Research Resources (P41-RR01081, P41RR001081)
- 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 › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- ERK2, PEA-15, Elk-1, protein-protein interaction, MAPK signaling, ERK2 phosphorylation
- MeSH terms
- Animals, Cell Nucleus, Cytoplasm, Fluorescence Polarization, Humans, Kinetics, Models, Biological, Models, Molecular, Phosphoproteins, Protein Binding, Protein Structure, Tertiary, Mitogen-Activated Protein Kinase 1, Active Transport, Cell Nucleus, Mitogen-Activated Protein Kinase 3, Apoptosis Regulatory Proteins
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Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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