Evidence map›Paper›PMID 27102985›Full record

ArticleThe Biochemical journal2016

AKAP18:PKA-RIIα structure reveals crucial anchor points for recognition of regulatory subunits of PKA.

Frank Götz, Yvette Roske, Maike Svenja Schulz, Karolin Autenrieth, Daniela Bertinetti, Katja Faelber, Kerstin Zühlke, Annika Kreuchwig, Eileen J Kennedy, Gerd Krause and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Disruptors of AKAP-Dependent Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  7. Article
  8. Review
  9. AKAP Signaling Islands: Venues for Precision Pharmacology.Trends in pharmacological sciences · 2020
    Review
  10. Article
  11. Review
  12. Review
  13. Single nucleotide polymorphisms alter kinase anchoring and the subcellular targeting of A-kinase anchoring proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Mechanisms for restraining cAMP-dependent protein kinase revealed by subunit quantitation and cross-linking approaches.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

14 authors at 4 institutions in 1 country.

Frank GötzMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Yvette RoskeMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Maike Svenja SchulzMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Karolin AutenriethDepartment of Biochemistry, University of Kassel, Heirnich-Plett-Str. 40, 34132 Kassel, Germany.
Daniela BertinettiDepartment of Biochemistry, University of Kassel, Heirnich-Plett-Str. 40, 34132 Kassel, Germany.
Katja FaelberMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Kerstin ZühlkeMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Annika KreuchwigLeibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Eileen J KennedyDepartment of Pharmaceutical and Biomedical Sciences, College of Pharmacy, University of Georgia, 240 W. Green St., Athens, GA 30602, U.S.A.
Gerd KrauseLeibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Oliver DaumkeMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Friedrich W HerbergDepartment of Biochemistry, University of Kassel, Heirnich-Plett-Str. 40, 34132 Kassel, Germany.
Udo HeinemannMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Enno KlussmannMax Delbrück Centre for Molecular Medicine Berlin in the Helmholtz Association (MDC), Robert-Rössle-Straße 10, 13125 Berlin, Germany DZHK, German Centre for Cardiovascular Research, Oudenarder Straße 16,13347 Berlin, Germany enno.klussmann@mdc-berlin.de.
Max Delbrück Center · DELeibniz Association · DEUniversity of Kassel · DEGerman Centre for Cardiovascular Research · DE

Funding

Targeted Inhibition of EGFR DimerizationR03CA188439 · NCI · UNIVERSITY OF GEORGIA · PI KENNEDY, EILEEN J · 2015 to 2016
$150k
NCI NIH HHS R03 CA188439
6 · The paper itself

Abstract

A-kinase anchoring proteins (AKAPs) interact with the dimerization/docking (D/D) domains of regulatory subunits of the ubiquitous protein kinase A (PKA). AKAPs tether PKA to defined cellular compartments establishing distinct pools to increase the specificity of PKA signalling. Here, we elucidated the structure of an extended PKA-binding domain of AKAP18β bound to the D/D domain of the regulatory RIIα subunits of PKA. We identified three hydrophilic anchor points in AKAP18β outside the core PKA-binding domain, which mediate contacts with the D/D domain. Such anchor points are conserved within AKAPs that bind regulatory RII subunits of PKA. We derived a different set of anchor points in AKAPs binding regulatory RI subunits of PKA. In vitro and cell-based experiments confirm the relevance of these sites for the interaction of RII subunits with AKAP18 and of RI subunits with the RI-specific smAKAP. Thus we report a novel mechanism governing interactions of AKAPs with PKA. The sequence specificity of each AKAP around the anchor points and the requirement of these points for the tight binding of PKA allow the development of selective inhibitors to unequivocally ascribe cellular functions to the AKAP18-PKA and other AKAP-PKA interactions.

Indexed as

A Kinase Anchor ProteinsAmino Acid SequenceBinding SitesCalorimetryCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansImmunoprecipitationMolecular Sequence DataProtein BindingProtein ConformationProtein SubunitsSignal TransductionSurface Plasmon ResonanceA Kinase Anchor ProteinsCyclic AMP-Dependent Protein KinasesProtein SubunitsA-kinase anchoring proteincompartmentalized cAMP signallingD/D domainPKA-binding domainprotein kinase Aprotein–protein interaction

Identifiers

PMID27102985
PMCPMC4964276
OpenAlexW2340282875

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.