Evidence map›Paper›PMID 20980620›Full record

ArticleMolecular biology of the cell2010

Polycystin-1 surface localization is stimulated by polycystin-2 and cleavage at the G protein-coupled receptor proteolytic site.

Hannah C Chapin, Vanathy Rajendran, Michael J Caplan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.7field-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

49 citing papers in PubMed, 79 citations in OpenAlex.

  1. AbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Glycosylation in kidney diseases.Precision clinical medicine · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The GPCR properties of polycystin-1- A new paradigm.Frontiers in molecular biosciences · 2022
    Review
  10. Review
  11. Polycystin-1 dependent regulation of polycystin-2 via GRP94, a member of HSP90 family that resides in the endoplasmic reticulum.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  12. Article
  13. Primary Cilia and Atherosclerosis.Frontiers in physiology · 2021
    Review
  14. Review
  15. Review
  16. Review
  17. Synergistic Genetic Interactions betweenJournal of the American Society of Nephrology : JASN · 2019
    Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Hannah C ChapinDepartments of Cell Biology and Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520, USA.
Vanathy Rajendran
Michael J Caplan
Yale University · US

Funding

YALE CENTER FOR THE STUDY OF POLYCYSTIC KIDNEY DISEASEP50DK057328 · NIDDK · YALE UNIVERSITY · PI SOMLO, STEFAN · 1999 to 2009
$11.1M
NIDDK NIH HHS DK-57328NIDDK NIH HHS P50 DK057328
6 · The paper itself

Abstract

Polycystin (PC)1 and PC2 are membrane proteins implicated in autosomal dominant polycystic kidney disease. A physiologically relevant cleavage at PC1's G protein-coupled receptor proteolytic site (GPS) occurs early in the secretory pathway. Our results suggest that PC2 increases both PC1 GPS cleavage and PC1's appearance at the plasma membrane. Mutations that prevent PC1's GPS cleavage prevent its plasma membrane localization. PC2 is a member of the trp family of cation channels and is an important PC1 binding partner. The effect of PC2 on PC1 localization is independent of PC2 channel activity, as tested using channel-inhibiting PC2 mutations. PC1 and PC2 can interact through their C-terminal tails, but removing the C-terminal tail of either protein has no effect on PC1 surface localization in human embryonic kidney 293 cells. Experiments in polarized LLC-PK cells show that apical and ciliary PC1 localization requires PC2 and that this delivery is sensitive to PC2 truncation. In sum, our work shows that PC2 expression is required for the movement of PC1 to the plasma and ciliary membranes. In fibroblast cells this localization effect is independent of PC2's channel activity or PC1 binding ability but involves a stimulation of PC1's GPS cleavage before the PC1 protein's surface delivery.

Indexed as

Protein Processing, Post-TranslationalAnimalsBlotting, WesternCell MembraneCiliaFluorescent Antibody TechniqueHEK293 CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMutationPolycystic Kidney, Autosomal DominantProtein BindingProtein IsoformsProtein Structure, TertiaryProtein IsoformsTRPP Cation Channels

Identifiers

PMID20980620
PMCPMC3002387
OpenAlexW2135389531

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.