Evidence map›Paper›PMID 26527685›Full record

ArticleThe Journal of biological chemistry2016

Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY.

Gergő Gógl, Anita Alexa, Bence Kiss, Gergely Katona, Mihály Kovács, Andrea Bodor, Attila Reményi, László Nyitray

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
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  13. Classifying the Binding Modes of Disordered Proteins.International journal of molecular sciences · 2020
    Review
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  16. Article
  17. Review
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  19. Article
  20. Structural Basis for S100B Interaction with its Target Proteins.Journal of molecular and genetic medicine : an international journal of biomedical research · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Gergő GóglFrom the Department of Biochemistry.
Anita Alexathe "Momentum" Protein Interaction Group, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary, and.
Bence KissFrom the Department of Biochemistry.
Gergely Katonathe Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden.
Mihály KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, and.
Andrea BodorInstitute of Chemistry Eötvös Loránd University, 1117 Budapest, Hungary.
Attila Reményithe "Momentum" Protein Interaction Group, Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary, and remenyi.attila@ttk.mta.hu.
László NyitrayFrom the Department of Biochemistry, nyitray@elte.hu.ORCID http://orcid.org/0000-0003-4717-5994
Institute of Molecular Life Sciences · HUEötvös Loránd University · HUUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPK) promote MAPK-activated protein kinase activation. In the MAPK pathway responsible for cell growth, ERK2 initiates the first phosphorylation event on RSK1, which is inhibited by Ca(2+)-binding S100 proteins in malignant melanomas. Here, we present a detailed in vitro biochemical and structural characterization of the S100B-RSK1 interaction. The Ca(2+)-dependent binding of S100B to the calcium/calmodulin-dependent protein kinase (CaMK)-type domain of RSK1 is reminiscent of the better known binding of calmodulin to CaMKII. Although S100B-RSK1 and the calmodulin-CAMKII system are clearly distinct functionally, they demonstrate how unrelated intracellular Ca(2+)-binding proteins could influence the activity of the CaMK domain-containing protein kinases. Our crystallographic, small angle x-ray scattering, and NMR analysis revealed that S100B forms a "fuzzy" complex with RSK1 peptide ligands. Based on fast-kinetics experiments, we conclude that the binding involves both conformation selection and induced fit steps. Knowledge of the structural basis of this interaction could facilitate therapeutic targeting of melanomas.

Indexed as

MAP Kinase Signaling SystemAmino Acid SequenceCalciumCrystallography, X-RayEnzyme ActivationExtracellular Signal-Regulated MAP KinasesFluorescence PolarizationKineticsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiaryRibosomal Protein S6 Kinases, 90-kDaS100 Calcium Binding Protein beta SubunitSolutionsStructure-Activity RelationshipCalciumExtracellular Signal-Regulated MAP KinasesRibosomal Protein S6 Kinases, 90-kDaS100 Calcium Binding Protein beta SubunitSolutionsTryptophancalciumcrystal structureextracellular-signal-regulated kinase (ERK)kineticsmelanomamitogen-activated protein kinase (MAPK)nuclear magnetic resonance (NMR)RSKS100 proteinssmall-angle X-ray scattering (SAXS)

Identifiers

PMID26527685
PMCPMC4697148
OpenAlexW2197515196

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.