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Cited by 15S100 Proteins and AnnexinsAdvanced Glycation End Products researchProtein Interaction Studies and Fluorescence Analysis

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Calcium-Bound S100P Protein Is a Promiscuous Binding Partner of the Four-Helical Cytokines

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Kazakov, Alexey S., Deryusheva, Evgenia I., Permyakova, Maria E., Sokolov, Andrey S., Rastrygina, Victoria A., Uversky, Vladimir N., Permyakov, Eugene A., Permyakov, Sergei E.·2022·International Journal of Molecular Sciences
DOI 10.3390/ijms231912000PMC PMC9569990

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Abstract

S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated by the recognition of specific receptor proteins. Recent studies indicate the ability of some S100 proteins to affect cytokine signaling through direct interaction with cytokines. S100P was shown to be the S100 protein most actively involved in interactions with some four-helical cytokines. To assess the selectivity of the S100P protein binding to four-helical cytokines, we have probed the interaction of Ca2+-bound recombinant human S100P with a panel of 32 four-helical human cytokines covering all structural families of this fold, using surface plasmon resonance spectroscopy. A total of 22 cytokines from all families of four-helical cytokines are S100P binders with the equilibrium dissociation constants, Kd, ranging from 1 nM to 3 µM (below the Kd value for the S100P complex with the V domain of its conventional receptor, receptor for advanced glycation end products, RAGE). Molecular docking and mutagenesis studies revealed the presence in the S100P molecule of a cytokine-binding site, which overlaps with the RAGE-binding site. Since S100 binding to four-helical cytokines inhibits their signaling in some cases, the revealed ability of the S100P protein to interact with ca. 71% of the four-helical cytokines indicates that S100P may serve as a poorly selective inhibitor of their action.

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Metadata

Authors
Kazakov, A. S., Deryusheva, E. I., Permyakova, M. E., Sokolov, A. S., Rastrygina, V. A., Uversky, V. N., Permyakov, E. A., & Permyakov, S. E.
Affiliations
Russian Academy of Sciences (RU)
Corresponding author
  • Uversky, Vladimir N.
  • Permyakov, Sergei E.
ORCID
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2022-10-09
Volume
23
Issue
19
Pages
12000
ISSN
1422-0067 (ISSN-L)
DOI
10.3390/ijms231912000
PMC
PMC9569990
OpenAlex
W4303946024
Cited by
15
References
2
Citations by year
2026: 6 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 1
FWCI
0.73
Type
journal article
Language
en
Open access
Licence
Locations
  • International Journal of Molecular Sciences (publishedVersion, cc-by)
  • Preprints.org (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Digital Commons - University of South Florida (University of South Florida) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Russian Science Foundation (№19-14-00289)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords
S100P, S-100 protein, calcium-binding proteins, cytokine signaling, protein-protein interaction, receptor for advanced glycation end products, RAGE, binding selectivity, cytokine signaling inhibition
MeSH terms
Receptor for Advanced Glycation End Products, Calcium, Calcium-Binding Proteins, Calcium, Dietary, Carrier Proteins, Humans, Immunologic Factors, Neoplasm Proteins, S100 Proteins, Protein Binding, Cytokines, Molecular Docking Simulation

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