Evidence map›Paper›PMID 32571882›Full record

ReviewThe Journal of biological chemistry2020

Structural insights into emergent signaling modes of G protein-coupled receptors.

Ieva Sutkeviciute, Jean-Pierre Vilardaga

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.4field-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

52 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  16. Ciliary G-Protein Coupled Receptor Signaling in Polycystic Kidney Disease.International journal of molecular sciences · 2025
    Review
  17. Review
  18. Article
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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.

Ieva SutkeviciuteLaboratory for GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA ies4@pitt.edu jpv@pitt.edu.
Jean-Pierre VilardagaLaboratory for GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA ies4@pitt.edu jpv@pitt.edu.ORCID 0000-0002-1217-1435
University of Pittsburgh · US

Funding

Structure and function of PTH class B GPCRR01DK116780 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Ivet Bahar, Jean-Pierre Vilardaga · 2018 to 2026
$4.2M
Functional Polarity of PTH Receptor Signaling: Cellular and Molecular MechanismsR01DK111427 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FRIEDMAN, PETER A, VILARDAGA, JEAN-PIERRE · 2017 to 2020
$2.4M
Regulation of Parathyroid Functions By G-Protein Coupled ReceptorsR01DK122259 · NIDDK · NORTHERN CALIFORNIA INSTITUTE/RES/EDU · PI CHANG, WENHAN, VILARDAGA, JEAN-PIERRE · 2019 to 2023
$2.2M
Skeletal Anabolism by Simultaneously Targeting the PTH1R and CaSRF30DE024952 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SANTA MARIA, CHRISTIAN YUZON · 2014 to 2019
$255k
NIDCR NIH HHS F30 DE024952NIDDK NIH HHS R01 DK111427NIDDK NIH HHS R01 DK116780NIDDK NIH HHS R01 DK122259
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) represent the largest family of cell membrane proteins, with >800 GPCRs in humans alone, and recognize highly diverse ligands, ranging from photons to large protein molecules. Very important to human medicine, GPCRs are targeted by about 35% of prescription drugs. GPCRs are characterized by a seven-transmembrane α-helical structure, transmitting extracellular signals into cells to regulate major physiological processes via heterotrimeric G proteins and β-arrestins. Initially viewed as receptors whose signaling via G proteins is delimited to the plasma membrane, it is now recognized that GPCRs signal also at various intracellular locations, and the mechanisms and (patho)physiological relevance of such signaling modes are actively investigated. The propensity of GPCRs to adopt different signaling modes is largely encoded in the structural plasticity of the receptors themselves and of their signaling complexes. Here, we review emerging modes of GPCR signaling via endosomal membranes and the physiological implications of such signaling modes. We further summarize recent structural insights into mechanisms of GPCR activation and signaling. We particularly emphasize the structural mechanisms governing the continued GPCR signaling from endosomes and the structural aspects of the GPCR resensitization mechanism and discuss the recently uncovered and important roles of lipids in these processes.

Indexed as

Signal TransductionAnimalsbeta-ArrestinsCyclic AMPEndosomesHumansMembrane LipidsModels, MolecularProtein ConformationReceptors, G-Protein-Coupledbeta-ArrestinsCyclic AMPMembrane LipidsReceptors, G-Protein-CoupledarrestincAMPcyclic AMP (cAMP)endosomal membraneendosomeenvironmental sensingG protein-coupled receptor (GPCR)membrane lipidparathyroid hormonereceptor structure-functionsignal transductionstructural dynamicsstructure-functionβ-arrestins

Identifiers

PMID32571882
PMCPMC7450137
OpenAlexW3036711312

What OpenQuestion holds

Textmetadata
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.