Evidence map›Paper›PMID 24022404›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2014

Myristoylated alanine-rich C kinase substrate coordinates native TRPC1 channel activation by phosphatidylinositol 4,5-bisphosphate and protein kinase C in vascular smooth muscle.

Jian Shi, Lutz Birnbaumer, William A Large, Anthony P Albert

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Role for the PIPJournal of cell communication and signaling · 2024
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Obligatory role for PKCδ in PIPThe Journal of physiology · 2020
    Article
  7. Review
  8. PIPProceedings of the National Academy of Sciences of the United States of America · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Store depletion induces Gαq-mediated PLCβ1 activity to stimulate TRPC1 channels in vascular smooth muscle cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  14. Review
  15. Article
  16. Review
  17. 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

4 authors at 2 institutions in 2 countries.

Jian Shi1Pharmacology and Cell Physiology, Division of Biomedical Sciences, St. George's, University of London, Cranmer Terrace, London SW17 0RE, UK. aalbert@sgul.ac.uk.
Lutz Birnbaumer
William A Large
Anthony P Albert
St George's, University of London · GBNational Institute of Environmental Health Sciences · US

Funding

Transmembrane Signaling MechanismsZIAES101643 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI BIRNBAUMER, LUTZ · 2011 to 2014
$5.4M
Transmembrane Signaling Mechanisms Involving TRP ChannelsZIAES101684 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI BIRNBAUMER, LUTZ · 2011 to 2014
$3.2M
Transmembrane Signaling Mechanisms Involving TRP ChannelsZ01ES101684 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI BIRNBAUMER, LUTZ · 2003 to 2008
$2.1M
Biotechnology and Biological Sciences Research Council BB/J007226/1Intramural NIH HHS Z01 ES101684NIEHS NIH HHS Z01-ES-101684
6 · The paper itself

Abstract

Canonical transient receptor potential 1 (TRPC1) Ca(2+)-permeable cation channels contribute to vascular tone and blood vessel remodeling and represent potential therapeutic targets for cardiovascular disease. Protein kinase C (PKC) and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] are obligatory for native TRPC1 channel activation in vascular smooth muscle cells (VSMCs) but how PKC and PI(4,5)P2 act together to induce channel gating remains unresolved. The present study reveals that myristoylated alanine-rich C kinase substrate (MARCKS) protein coordinates activation of TRPC1 channels by PKC and PI(4,5)P2. TRPC1 channels and MARCKS form signaling complexes with PI(4,5)P2 bound to MARCKS; in this configuration TRPC1 channels are closed. Activators of TRPC1 channels induce PKC phosphorylation of TRPC1 proteins, which causes dissociation of TRPC1 subunits from MARCKS and release of PI(4,5)P2 from MARCKS; PI(4,5)P2 subsequently binds to TRPC1 subunits to induce channel opening. Calmodulin acting at, or upstream of, MARCKS is also required for TRPC1 channel opening through a similar gating mechanism involving PKC and PI(4,5)P2. These novel findings show that MARCKS coordinates native TRPC1 channel activation in VSMCs by acting as a reversible PI(4,5)P2 buffer, which is regulated by PKC-mediated TRPC1 phosphorylation. Moreover, our data provide evidence that PI(4,5)P2 is a gating ligand of TRPC1 channels.

Indexed as

AnimalsIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMuscle, Smooth, VascularMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylinositol 4,5-DiphosphateProtein Kinase CRabbitsTRPC Cation ChannelsIntracellular Signaling Peptides and ProteinsMarcks protein, mouseMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylinositol 4,5-DiphosphateProtein Kinase Ctransient receptor potential cation channel, subfamily C, member 1TRPC Cation ChannelsCa2+ signalingcalmodulintransgenic

Identifiers

PMID24022404
PMCPMC3868830
OpenAlexW2014954303

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.