Evidence map›Paper›PMID 23115245›Full record

Trial reportThe Journal of biological chemistry2012

A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase A-regulatory subunit I (PKA-RI) to the plasma membrane.

Pepijn P Burgers, Yuliang Ma, Luigi Margarucci, Mason Mackey, Marcel A G van der Heyden, Mark Ellisman, Arjen Scholten, Susan S Taylor, Albert J R Heck

Open access · hybridAbstract readClinical Trial
In one paragraph

Trial report in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 88 citations in OpenAlex.

  1. Regulation of Translation by PKA Signaling Pathway.International journal of molecular sciences · 2026
    Review
  2. Review
  3. N3A motifs in RIβ mediate allosteric crosstalk between cAMP and ATP in PKA activation.Protein science : a publication of the Protein Society · 2025
    Article
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  5. Article
  6. Review
  7. Article
  8. Article
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  11. Article
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  13. Article
  14. Review
  15. Protein Kinase A Detection in Human Urine Samples.Journal of clinical medicine · 2021
    Article
  16. Review
  17. Review
  18. Review
  19. AKAP Signaling Islands: Venues for Precision Pharmacology.Trends in pharmacological sciences · 2020
    Review
  20. Review
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

9 authors at 5 institutions in 3 countries.

Pepijn P BurgersBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Yuliang Ma
Luigi Margarucci
Mason Mackey
Marcel A G van der Heyden
Mark Ellisman
Arjen Scholten
Susan S Taylor
Albert J R Heck
University of California, San Diego · USUtrecht University · NLHoward Hughes Medical Institute · USUniversity Medical Center Utrecht · NLUniversity of Salerno · IT

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
Howard Hughes Medical InstituteNIDDK NIH HHS DK54441NIDDK NIH HHS P01 DK054441
6 · The paper itself

Abstract

Protein kinase A-anchoring proteins (AKAPs) provide spatio-temporal specificity for the omnipotent cAMP-dependent protein kinase (PKA) via high affinity interactions with PKA regulatory subunits (PKA-RI, RII). Many PKA-RII-AKAP complexes are heavily tethered to cellular substructures, whereas PKA-RI-AKAP complexes have remained largely undiscovered. Here, using a cAMP affinity-based chemical proteomics strategy in human heart and platelets, we uncovered a novel, ubiquitously expressed AKAP, termed small membrane (sm)AKAP due to its specific localization at the plasma membrane via potential myristoylation/palmitoylation anchors. In vitro binding studies revealed specificity of smAKAP for PKA-RI (K(d) = 7 nM) over PKA-RII (K(d) = 53 nM) subunits, co-expression of smAKAP with the four PKA R subunits revealed an even more exclusive specificity of smAKAP for PKA-RIα/β in the cellular context. Applying the singlet oxygen-generating electron microscopy probe miniSOG indicated that smAKAP is tethered to the plasma membrane and is particularly dense at cell-cell junctions and within filopodia. Our preliminary functional characterization of smAKAP provides evidence that, like PKA-RII, PKA-RI can be tightly tethered by a novel repertoire of AKAPs, providing a new perspective on spatio-temporal control of cAMP signaling.

Indexed as

A Kinase Anchor ProteinsAnimalsCell MembraneCyclic AMPCyclic AMP-Dependent Protein Kinase Type IFemaleHumansIntercellular JunctionsLipoylationMaleMiceProtein BindingPseudopodiaSecond Messenger SystemsA Kinase Anchor ProteinsCyclic AMPCyclic AMP-Dependent Protein Kinase Type I

Identifiers

PMID23115245
PMCPMC3527963
OpenAlexW2027282106

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.