ArticleProtein science : a publication of the Protein Society1998
S100B(betabeta) inhibits the protein kinase C-dependent phosphorylation of a peptide derived from p53 in a Ca2+-dependent manner.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 71 citations in OpenAlex.
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
- Computational Design of Macrocyclic Binders of S100B(ββ): Novel Peptide Theranostics.Molecules (Basel, Switzerland) · 2021Article
- Emerging Biomarkers in Cutaneous Melanoma.Molecular diagnosis & therapy · 2018Review
- Structural Basis for S100B Interaction with its Target Proteins.Journal of molecular and genetic medicine : an international journal of biomedical research · 2018Article
- A New Technique for Collection of Cerebrospinal Fluid in Rat Pups.Journal of experimental neuroscience · 2015Article
- Covalent small molecule inhibitors of Ca(2+)-bound S100B.Biochemistry · 2014Article
- Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin.Protein science : a publication of the Protein Society · 2014Article
- Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide.Biopolymers · 2014Article
- Complex formation between S100B protein and the p90 ribosomal S6 kinase (RSK) in malignant melanoma is calcium-dependent and inhibits extracellular signal-regulated kinase (ERK)-mediated phosphorylation of RSK.The Journal of biological chemistry · 2014Article
- The evolution of S100B inhibitors for the treatment of malignant melanoma.Future medicinal chemistry · 2013Review
- Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B.Biochemistry · 2012Article
- Insight into a novel p53 single point mutation (G389E) by Molecular Dynamics Simulations.International journal of molecular sciences · 2010Article
- In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction.International journal of high throughput screening · 2010Article
- The effect of pentamidine on melanoma ex vivo.Anti-cancer drugs · 2010Article
- The Calcium-Dependent Interaction of S100B with Its Protein Targets.Cardiovascular psychiatry and neurology · 2010Article
- Tumor cell and circulating markers in melanoma: diagnosis, prognosis, and management.Current oncology reports · 2005Review
- A logical sequence search for S100B target proteins.Protein science : a publication of the Protein Society · 2000Article
- Structural changes in the C-terminus of Ca2+-bound rat S100B (beta beta) upon binding to a peptide derived from the C-terminal regulatory domain of p53.Protein science : a publication of the Protein Society · 1999Article
- The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).Protein science : a publication of the Protein Society · 1999Article
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4 authors at 1 institution in 1 country.
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Abstract
S100B(betabeta) is a dimeric Ca2+-binding protein that is known to inhibit the protein kinase C (PKC)-dependent phosphorylation of several proteins. To further characterize this inhibition, we synthesized peptides based on the PKC phosphorylation domains of p53 (residues 367-388), neuromodulin (residues 37-53), and the regulatory domain of PKC (residues 19-31), and tested them as substrates for PKC. All three peptides were shown to be good substrates for the catalytic domain of PKC. As for full-length p53 (Baudier J, Delphin C, Grunwald D, Khochbin S, Lawrence JJ. 1992. Proc Natl Acad Sci USA 89:11627-11631), S100B(betabeta) binds the p53 peptide and inhibits its PKC-dependent phosphorylation (IC50 = 10 +/- 7 microM) in a Ca2+-dependent manner. Similarly, phosphorylation of the neuromodulin peptide and the PKC regulatory domain peptide were inhibited by S100B(betabeta) in the presence of Ca2+ (IC50 = 17 +/- 5 microM; IC50 = 1 +/- 0.5 microM, respectively). At a minimum, the C-terminal EF-hand Ca2+-binding domain (residues 61-72) of each S100beta subunit must be saturated to inhibit phosphorylation of the p53 peptide as determined by comparing the Ca2+ dependence of inhibition ([Ca]IC50 = 29.3 +/- 17.6 microM) to the dissociation of Ca2+ from the C-terminal EF-hand Ca2+-binding domain of S100B(betabeta).
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