Evidence map›Paper›PMID 36763973›Full record

ReviewAnnual review of physiology2023

Polycystin Channel Complexes.

Orhi Esarte Palomero, Megan Larmore, Paul G DeCaen

Open access · hybridAbstract readReview
In one paragraph

Review in Annual review of physiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
12.8field-weighted citation impact, top 1% 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

31 citing papers in PubMed, 41 citations in OpenAlex.

  1. PKD2-like proteins targetProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
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  6. Article
  7. Review
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  12. Review
  13. 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
  14. Hyperosmolality activates polycystin-2 and TRPM4 in renal primary cilium.Pflugers Archiv : European journal of physiology · 2025
    Article
  15. Article
  16. Article
  17. The mutual interaction of TRPC5 channel with polycystin proteins.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
    Article
  18. Article
  19. A synthetic method to assay polycystin channel biophysics.bioRxiv : the preprint server for biology · 2024
    Article
  20. Calcium signalling and transport in the kidney.Nature reviews. Nephrology · 2024
    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

3 authors at 1 institution in 1 country.

Orhi Esarte PalomeroDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA; email: paul.decaen@northwestern.edu.
Megan LarmoreDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA; email: paul.decaen@northwestern.edu.
Paul G DeCaenDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA; email: paul.decaen@northwestern.edu.
Northwestern University · US

Funding

Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Training Core for Chicago KUH FORWARDTL1DK132769 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Tamara Isakova · 2021 to 2026
$4.0M
Professional Development Core for Chicago KUH FORWARDU2CDK129917 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SUSAN E. QUAGGIN · 2021 to 2026
$2.9M
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
Cilia calcium dysregulation in polycystic kidney diseaseR01DK131118 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Paul Gregory DeCaen · 2022 to 2026
$1.9M
NIDDK NIH HHS R01 DK123463NIDDK NIH HHS R01 DK131118NIDDK NIH HHS TL1 DK132769NIDDK NIH HHS U2C DK129917NIGMS NIH HHS T32 GM008382
6 · The paper itself

Abstract

Polycystin subunits can form hetero- and homotetrameric ion channels in the membranes of various compartments of the cell. Homotetrameric polycystin channels are voltage- and calcium-modulated, whereas heterotetrameric versions are proposed to be ligand- or autoproteolytically regulated. Their importance is underscored by variants associated with autosomal dominant polycystic kidney disease and by vital roles in fertilization and embryonic development. The diversity in polycystin assembly and subcellular distribution allows for a multitude of sensory functions by this class of channels. In this review, we highlight their recent structural and functional characterization, which has provided a molecular blueprint to investigate the conformational changes required for channel opening in response to unique stimuli. We consider each polycystin channel type individually, discussing how they contribute to sensory cell biology, as well as their impact on the physiology of various tissues.

Indexed as

TRPP Cation ChannelsCalciumHumansSignal TransductionCalciumTRPP Cation ChannelsADPKDautosomal dominant polycystic kidney diseaseciliopathiesgating mechanismpolycystinprimary ciliaTRP channel

Identifiers

PMID36763973
PMCPMC10029091
OpenAlexW4319881080

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.