Evidence map›Paper›PMID 30353650›Full record

ReviewTraffic (Copenhagen, Denmark)2019

Endo-lysosomal sorting of G-protein-coupled receptors by ubiquitin: Diverse pathways for G-protein-coupled receptor destruction and beyond.

Michael R Dores, JoAnn Trejo

Open access · bronzeAbstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.6field-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

28 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  6. Review
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  13. Cathepsin D interacts with adenosine AThe Journal of biological chemistry · 2022
    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 2 institutions in 1 country.

Michael R DoresDepartment of Biology, Hofstra University, Hempstead, New York.ORCID 0000-0001-9243-0582
JoAnn TrejoDepartment of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, California.ORCID 0000-0003-4405-6228
Hofstra University · USUniversity of California San Diego · US

Funding

UCSD/SDSU IRACDAK12GM068524 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TREJO, JOANN · 2003 to 2025
$24.4M
Cell Signaling by Protease-activated G Protein-coupled ReceptorsR35GM127121 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Joann Trejo · 2018 to 2026
$4.5M
Mechanisms Regulating GPCR TraffickingR01GM090689 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TREJO, JOANN · 2010 to 2018
$2.9M
GPCR Cytoprotective Signaling MechanismsR01GM116597 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHI, NEIL C, TREJO, JOANN · 2015 to 2018
$1.7M
Addressing Racial Disparities in Influenza PreventionK01IP000050 · IP · NORTHWESTERN UNIVERSITY · PI CAMERON, KENZIE A · 2004 to 2005
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NCIRD CDC HHS K01 IP000050NIGMS NIH HHS K12 GM068524NIGMS NIH HHS R01 GM090689NIGMS NIH HHS R01 GM116597NIGMS NIH HHS R35 GM127121NIH HHS NIGMS R35 GM127121
6 · The paper itself

Abstract

Ubiquitin is covalently attached to substrate proteins in the form of a single ubiquitin moiety or polyubiquitin chains and has been generally linked to protein degradation, however, distinct types of ubiquitin linkages are also used to control other critical cellular processes like cell signaling. Over forty mammalian G protein-coupled receptors (GPCRs) have been reported to be ubiquitinated, but despite the diverse and rich complexity of GPCR signaling, ubiquitin has been largely ascribed to receptor degradation. Indeed, GPCR ubiquitination targets the receptors for degradation by lysosome, which is mediated by the Endosomal Sorting Complexes Required for Transport (ESCRT) machinery, and the proteasome. This has led to the view that ubiquitin and ESCRTs primarily function as the signal to target GPCRs for destruction. Contrary to this conventional view, studies indicate that ubiquitination of certain GPCRs and canonical ubiquitin-binding ESCRTs are not required for receptor degradation and revealed that diverse and complex pathways exist to regulate endo-lysosomal sorting of GPCRs. In other studies, GPCR ubiquitination has been shown to drive signaling and not receptor degradation and further revealed novel insight into the mechanisms by which GPCRs trigger the activity of the ubiquitination machinery. Here, we discuss the diverse pathways by which ubiquitin controls GPCR endo-lysosomal sorting and beyond.

Indexed as

UbiquitinationAnimalsEndosomal Sorting Complexes Required for TransportEndosomesHumansLysosomesProtein TransportReceptors, G-Protein-CoupledEndosomal Sorting Complexes Required for TransportReceptors, G-Protein-CoupledALIXARRDC3E3 ligasesESCRTexosomesG proteinHRSNEDD4PAR1β-Arrestins

Identifiers

PMID30353650
PMCPMC6385894
OpenAlexW2898498783

What Socratic 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 Socratic graph.