Evidence map›Paper›PMID 26805887›Full record

ReviewCells2016

The Role of G-Protein-Coupled Receptor Proteolysis Site Cleavage of Polycystin-1 in Renal Physiology and Polycystic Kidney Disease.

Marie Trudel, Qin Yao, Feng Qian

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Mechanism of tethered agonist-mediated signaling by polycystin-1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Ligands and Beyond: Mechanosensitive Adhesion GPCRs.Pharmaceuticals (Basel, Switzerland) · 2022
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  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

3 authors at 2 institutions in 2 countries.

Marie TrudelMolecular Genetics and Development, Institut de Recherches Cliniques de Montreal, Universite de Montreal, Faculte de Medecine, Montréal, Québec H2W 1R7, Canada. marie.trudel@ircm.qc.ca.
Qin YaoDepartment of Medicine, Division of Nephrology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. qyao@medicine.umaryland.edu.
Feng QianDepartment of Medicine, Division of Nephrology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. fqian@medicine.umaryland.edu.
University of Maryland, Baltimore · USMontreal Clinical Research Institute · CA

Funding

Research BaseP30DK090868 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI WATNICK, TERRY J · 2010 to 2019
$11.1M
NIDDK NIH HHS P30 DK090868
6 · The paper itself

Abstract

Polycystin-1 (PC1) plays an essential role in renal tubular morphogenesis, and PC1 dysfunction causes human autosomal dominant polycystic kidney disease. A fundamental characteristic of PC1 is post-translational modification via cleavage at the juxtamembrane GPCR proteolysis site (GPS) motif that is part of the larger GAIN domain. Given the considerable biochemical complexity of PC1 molecules generated in vivo by this process, GPS cleavage has several profound implications on the intracellular trafficking and localization in association with their particular function. The critical nature of GPS cleavage is further emphasized by the increasing numbers of PKD1 mutations that significantly affect this cleavage process. The GAIN domain with the GPS motif therefore represents the key structural element with fundamental importance for PC1 and might be polycystic kidney disease's (PKD) Achilles' heel in a large spectrum of PKD1 missense mutations. We highlight the central roles of PC1 cleavage for the regulation of its biogenesis, intracellular trafficking and function, as well as its significance in polycystic kidney disease.

Indexed as

adhesion GPCRcis-autoproteolysisGAIN domainGPS motifpolycystic kidney diseasepolycystin

Identifiers

PMID26805887
PMCPMC4810088
OpenAlexW2283563018

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.