Evidence map›Paper›PMID 32305667›Full record

ReviewCellular signalling2020

Adhesion GPCRs as a paradigm for understanding polycystin-1 G protein regulation.

Robin L Maser, James P Calvet

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  11. Mechanism of tethered agonist-mediated signaling by polycystin-1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. The GPCR properties of polycystin-1- A new paradigm.Frontiers in molecular biosciences · 2022
    Review
  13. Article
  14. Review
  15. Review
  16. 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

2 authors at 1 institution in 1 country.

Robin L MaserDepartment of Clinical Laboratory Sciences, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, Kansas 66160, USA; Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, Kansas 66160, USA; Jared Grantham Kidney Institute, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, Kansas 66160, USA. Electronic address: rmaser@kumc.edu.
James P CalvetDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, Kansas 66160, USA; Jared Grantham Kidney Institute, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, Kansas 66160, USA. Electronic address: jcalvet@kumc.edu.
University of Kansas Medical Center · US

Funding

Pilot and Feasibility CoreP30DK106912 · NIDDK · UNIVERSITY OF KANSAS MEDICAL CENTER · PI CALVET, JAMES P · 2015 to 2019
$5.5M
Understanding Polycystin-1 Structure-GPCR Function for the Development of New Therapeutic Approaches in ADPKDR01DK123590 · NIDDK · UNIVERSITY OF KANSAS MEDICAL CENTER · PI MASER, ROBIN LEE · 2020 to 2023
$1.5M
NIDDK NIH HHS P30 DK106912NIDDK NIH HHS R01 DK123590
6 · The paper itself

Abstract

Polycystin-1, whose mutation is the most frequent cause of autosomal dominant polycystic kidney disease, is an extremely large and multi-faceted membrane protein whose primary or proximal cyst-preventing function remains undetermined. Accumulating evidence supports the idea that modulation of cellular signaling by heterotrimeric G proteins is a critical function of polycystin-1. The presence of a cis-autocatalyzed, G protein-coupled receptor (GPCR) proteolytic cleavage site, or GPS, in its extracellular N-terminal domain immediately preceding the first transmembrane domain is one of the notable conserved features of the polycystin-1-like protein family, and also of the family of cell adhesion GPCRs. Adhesion GPCRs are one of five families within the GPCR superfamily and are distinguished by a large N-terminal extracellular region consisting of multiple adhesion modules with a GPS-containing GAIN domain and bimodal functions in cell adhesion and signal transduction. Recent advances from studies of adhesion GPCRs provide a new paradigm for unraveling the mechanisms by which polycystin-1-associated G protein signaling contributes to the pathogenesis of polycystic kidney disease. This review highlights the structural and functional features shared by polycystin-1 and the adhesion GPCRs and discusses the implications of such similarities for our further understanding of the functions of this complicated protein.

Indexed as

AnimalsCell AdhesionGTP-Binding ProteinsHumansModels, BiologicalReceptors, G-Protein-CoupledSignal TransductionTRPP Cation ChannelsGTP-Binding ProteinsReceptors, G-Protein-CoupledTRPP Cation ChannelsADPKDCell adhesionGAIN domainGPSHeterotrimeric G protein

Identifiers

PMID32305667
PMCPMC7485580
OpenAlexW3017291948

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.