Evidence map›Paper›PMID 28423323›Full record

ArticleCell reports2017

Liberated PKA Catalytic Subunits Associate with the Membrane via Myristoylation to Preferentially Phosphorylate Membrane Substrates.

Shane E Tillo, Wei-Hong Xiong, Maho Takahashi, Sheng Miao, Adriana L Andrade, Dale A Fortin, Guang Yang, Maozhen Qin, Barbara F Smoody, Philip J S Stork and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 77 citations in OpenAlex.

  1. A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Sensitive and Selective Next-Generation FRET-based PKA Biosensors.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Structural determinants of protein kinase A essential for CFTR channel activation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

11 authors at 2 institutions in 1 country.

Shane E TilloVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Wei-Hong XiongVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Maho TakahashiVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Sheng MiaoVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Adriana L AndradeVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Dale A FortinVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Guang YangVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Maozhen QinVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Barbara F SmoodyVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Philip J S StorkVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA.
Haining ZhongVollum Institute, Oregon Health and Science University, Portland, OR 97239, USA. Electronic address: zhong@ohsu.edu.
Oregon Health & Science University · USVollum Institute · US

Funding

Examining the architecture of synapses in brain tissue at nanometer resolutionDP2OD008425 · OD · OREGON HEALTH & SCIENCE UNIVERSITY · PI ZHONG, HAINING · 2011 to 2011
$2.3M
A novel approach to examine slow synaptic transmission in vivoU01NS094247 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MAO, TIANYI, ZHONG, HAINING · 2015 to 2018
$1.3M
Spatial control of cAMP signaling by EpacsR01DK090309 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI STORK, PHILIP J.S. · 2011 to 2014
$1.1M
Mechanisms governing the compartmentalization of activated PKAF31NS079083 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI TILLO, SHANE · 2012 to 2014
$98k
NIDDK NIH HHS R01 DK090309NIH HHS DP2 OD008425NINDS NIH HHS F31 NS079083NINDS NIH HHS U01 NS094247
6 · The paper itself

Abstract

Protein kinase A (PKA) has diverse functions in neurons. At rest, the subcellular localization of PKA is controlled by A-kinase anchoring proteins (AKAPs). However, the dynamics of PKA upon activation remain poorly understood. Here, we report that elevation of cyclic AMP (cAMP) in neuronal dendrites causes a significant percentage of the PKA catalytic subunit (PKA-C) molecules to be released from the regulatory subunit (PKA-R). Liberated PKA-C becomes associated with the membrane via N-terminal myristoylation. This membrane association does not require the interaction between PKA-R and AKAPs. It slows the mobility of PKA-C and enriches kinase activity on the membrane. Membrane-residing PKA substrates are preferentially phosphorylated compared to cytosolic substrates. Finally, the myristoylation of PKA-C is critical for normal synaptic function and plasticity. We propose that activation-dependent association of PKA-C renders the membrane a unique PKA-signaling compartment. Constrained mobility of PKA-C may synergize with AKAP anchoring to determine specific PKA function in neurons.

Indexed as

A Kinase Anchor ProteinsAnimalsCell MembraneCyclic AMP-Dependent Protein Kinase Catalytic SubunitsCytosolEnzyme ActivationHEK293 CellsHumansMyristic AcidNeuronal PlasticityNeuronsPhosphorylationProtein BindingRatsSubstrate SpecificitySynapsesA Kinase Anchor ProteinsCyclic AMP-Dependent Protein Kinase Catalytic SubunitsMyristic Acidactivation-dependent membrane associationAMPA/NMDA current radiocAMP-dependent kinasediffusionmEPSCmobilitymyristoylationPKAsynaptic plasticity

Identifiers

PMID28423323
PMCPMC5481286
OpenAlexW2605804656

What OpenQuestion holds

Textmetadata
LicenceTDM
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.