Evidence map›Paper›PMID 26269590›Full record

ArticleThe Journal of biological chemistry2015

The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function.

María del Rocío Cantero, Irina F Velázquez, Andrew J Streets, Albert C M Ong, Horacio F Cantiello

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Paralog-specific TTC30 regulation of Sonic hedgehog signaling.Frontiers in molecular biosciences · 2023
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Cross-Talk Between the Adenylyl Cyclase/cAMP Pathway and CaReviews of physiology, biochemistry and pharmacology · 2021
    Review
  10. Review
  11. The Ion Channel and GPCR Toolkit of Brain Capillary Pericytes.Frontiers in cellular neuroscience · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

5 authors at 2 institutions in 2 countries.

María del Rocío CanteroFrom the Cátedra de Biofísica, Facultad de Odontología, Universidad de Buenos Aires, C1122AAH Buenos Aires, Argentina and.
Irina F VelázquezFrom the Cátedra de Biofísica, Facultad de Odontología, Universidad de Buenos Aires, C1122AAH Buenos Aires, Argentina and.
Andrew J StreetsKidney Genetics Group, Academic Nephrology Unit, The Henry Wellcome Laboratories for Medical Research, University of Sheffield Medical School, Sheffield S10 2RX, United Kingdom.
Albert C M OngKidney Genetics Group, Academic Nephrology Unit, The Henry Wellcome Laboratories for Medical Research, University of Sheffield Medical School, Sheffield S10 2RX, United Kingdom a.ong@sheffield.ac.uk.
Horacio F CantielloFrom the Cátedra de Biofísica, Facultad de Odontología, Universidad de Buenos Aires, C1122AAH Buenos Aires, Argentina and hcantiello@yahoo.com.ar.
University of Buenos Aires · ARUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polycystin-2 (PC2) is a TRP-type, Ca(2+)-permeable non-selective cation channel that plays an important role in Ca(2+) signaling in renal and non-renal cells. The effect(s) of the cAMP pathway and kinase mediated phosphorylation of PC2 seem to be relevant to PC2 trafficking and its interaction with polycystin-1. However, the role of PC2 phosphorylation in channel function is still poorly defined. Here we reconstituted apical membranes of term human syncytiotrophoblast (hST), containing endogenous PC2 (PC2hst), and in vitro translated channel protein (PC2iv). Addition of the catalytic subunit of PKA increased by 566% the spontaneous PC2hst channel activity in the presence of ATP. Interestingly, 8-Br-cAMP also stimulated spontaneous PC2hst channel activity in the absence of the exogenous kinase. Either stimulation was inhibited by addition of alkaline phosphatase, which in turn, was reversed by the phosphatase inhibitor vanadate. Neither maneuver modified the single channel conductance but instead increased channel mean open time. PKA directly phosphorylated PC2, which increased the mean open time but not the single channel conductance of the channel. PKA phosphorylation did not modify either R742X truncated or S829A-mutant PC2iv channel function. The data indicate that the cAMP pathway regulates PC2-mediated cation transport in the hST. The relevant PKA site for PC2 channel regulation centers on a single residue serine 829, in the carboxyl terminus.

Indexed as

Amino Acid SubstitutionCells, CulturedCyclic AMPCyclic AMP-Dependent Protein KinasesHumansIon TransportMutation, MissensePhosphorylationSecond Messenger SystemsTrophoblastsTRPP Cation ChannelsCyclic AMPCyclic AMP-Dependent Protein KinasesTRPP Cation Channelscyclic AMP (cAMP)electrophysiologyplacentaprotein kinase A (PKA)transient receptor potential channels (TRP channels)

Identifiers

PMID26269590
PMCPMC4583051
OpenAlexW2399541740

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.