Evidence map›Paper›PMID 22802962›Full record

ArticlePloS one2012

Structural interaction and functional regulation of polycystin-2 by filamin.

Qian Wang, Xiao-Qing Dai, Qiang Li, Zuocheng Wang, María del Rocío Cantero, Shu Li, Ji Shen, Jian-Cheng Tu, Horacio Cantiello, Xing-Zhen Chen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Function and regulation of TRPP2 ion channel revealed by a gain-of-function mutant.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Article
  10. The primary cilium calcium channels and their role in flow sensing.Pflugers Archiv : European journal of physiology · 2015
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. 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

10 authors at 5 institutions in 4 countries.

Qian WangMembrane Protein Disease Research Group, Department of Physiology, University of Alberta, Edmonton, Alberta, Canada.
Xiao-Qing Dai
Qiang Li
Zuocheng Wang
María del Rocío Cantero
Shu Li
Ji Shen
Jian-Cheng Tu
Horacio Cantiello
Xing-Zhen Chen
University of Alberta · CAMassachusetts General Hospital · USUniversity of Buenos Aires · ARWuhan University · CNZhongnan Hospital of Wuhan University · CN

Funding

Molecular Physiology of Polycystin-2R01DK077079 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI CANTIELLO, HORACIO F · 2009 to 2010
$733k
CIHRNIDDK NIH HHS DK077079NIDDK NIH HHS R01 DK077079
6 · The paper itself

Abstract

Filamins are important actin cross-linking proteins implicated in scaffolding, membrane stabilization and signal transduction, through interaction with ion channels, receptors and signaling proteins. Here we report the physical and functional interaction between filamins and polycystin-2, a TRP-type cation channel mutated in 10-15% patients with autosomal dominant polycystic kidney disease. Yeast two-hybrid and GST pull-down experiments demonstrated that the C-termini of filamin isoforms A, B and C directly bind to both the intracellular N- and C-termini of polycystin-2. Reciprocal co-immunoprecipitation experiments showed that endogenous polycystin-2 and filamins are in the same complexes in renal epithelial cells and human melanoma A7 cells. We then examined the effect of filamin on polycystin-2 channel function by electrophysiology studies with a lipid bilayer reconstitution system and found that filamin-A substantially inhibits polycystin-2 channel activity. Our study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein.

Indexed as

AnimalsCalcium ChannelsCell LineCell Line, TumorContractile ProteinsFilaminsHumansImmunoprecipitationLipid BilayersMicrofilament ProteinsProtein IsoformsTRPP Cation ChannelsTwo-Hybrid System TechniquesCalcium ChannelsContractile ProteinsFilaminsLipid BilayersMicrofilament ProteinsProtein IsoformsTRPP Cation Channels

Identifiers

PMID22802962
PMCPMC3393660
OpenAlexW1997958675

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.