Evidence map›Paper›PMID 32251715›Full record

ReviewCellular signalling2020

Structure and function of polycystin channels in primary cilia.

Chau My Ta, Thuy N Vien, Leo C T Ng, Paul G DeCaen

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular signalling, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
4.5field-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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Pathogenic variants in the polycystin pore helix cause distinct forms of channel dysfunction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Calcium signalling and transport in the kidney.Nature reviews. Nephrology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Chau My TaDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, 320 E Superior, Chicago, IL 60611, USA.
Thuy N VienDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, 320 E Superior, Chicago, IL 60611, USA.
Leo C T NgDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, 320 E Superior, Chicago, IL 60611, USA.
Paul G DeCaenDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, 320 E Superior, Chicago, IL 60611, USA. Electronic address: paul.decaen@northwestern.edu.
Northwestern University · US

Funding

Molecular dysregulation of primary cilia TRPP2 channels caused by Finger 1 variantsR01DK123463 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DECAEN, PAUL GREGORY · 2019 to 2023
$2.0M
The genetic identity of the primary cilia ion channels of kidney collecting duct cells and their regulation by internal calciumR00DK106655 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DECAEN, PAUL GREGORY · 2017 to 2019
$742k
The mechanistic impact of Finger 1 variants on polycystin-2 (PKD2) channels in the primary ciliaR56DK119709 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DECAEN, PAUL GREGORY · 2018 to 2018
$138k
NIDDK NIH HHS R00 DK106655NIDDK NIH HHS R01 DK123463NIDDK NIH HHS R56 DK119709
6 · The paper itself

Abstract

Variants in genes which encode for polycystin-1 and polycystin-2 cause most forms of autosomal dominant polycystic disease (ADPKD). Despite our strong understanding of the genetic determinants of ADPKD, we do not understand the structural features which govern the function of polycystins at the molecular level, nor do we understand the impact of most disease-causing variants on the conformational state of these proteins. These questions have remained elusive because polycystins localize to several organelle membranes, including the primary cilia. Primary cilia are microtubule based organelles which function as cellular antennae. Polycystin-2 and related polycystin-2 L1 are members of the transient receptor potential (TRP) ion channel family, and form distinct ion channels in the primary cilia of disparate cell types which can be directly measured. Polycystin-1 has both ion channel and adhesion G-protein coupled receptor (GPCR) features-but its role in forming a channel complex or as a channel subunit chaperone is undetermined. Nonetheless, recent polycystin structural determination by cryo-EM has provided a molecular template to understand their biophysical regulation and the impact of disease-causing variants. We will review these advances and discuss hypotheses regarding the regulation of polycystin channel opening by their structural domains within the context of the primary cilia.

Indexed as

AnimalsCalcium SignalingCiliaDisease ProgressionHumansProtein DomainsTRPP Cation ChannelsTRPP Cation Channels

Identifiers

PMID32251715
PMCPMC7373203
OpenAlexW3014393039

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.