Evidence map›Paper›PMID 37223976›Full record

ArticleMolecular biology of the cell2023

Divergent regulation of α-arrestin ARRDC3 function by ubiquitination.

Helen Wedegaertner, Oye Bosompra, Irina Kufareva, JoAnn Trejo

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Resident CD49aScience advances · 2026
    Article
  2. Article
  3. Association ofF1000Research · 2022
    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

4 authors at 1 institution in 1 country.

Helen WedegaertnerDepartment of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA92093.
Oye BosompraDepartment of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA92093.
Irina KufarevaDepartment of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA92093.
JoAnn TrejoDepartment of Pharmacology, School of Medicine, University of California, San Diego, La Jolla, CA92093.ORCID 0000-0003-4405-6228
University of California San Diego · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007198 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHI, NEIL C, INSEL, PAUL A · 1985 to 2024
$29.3M
GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Cell Signaling by Protease-activated G Protein-coupled ReceptorsR35GM127121 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Joann Trejo · 2018 to 2026
$4.5M
It's a tug of war: structure, consequences, and inhibition of CXCR4 and ACKR3 responses to lymphocyte chemoattractant CXCL12R01AI161880 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M, KUFAREVA, IRINA · 2021 to 2025
$3.4M
Signaling circuits that drive cell movement and ligand scavenging by chemokine receptor CCR2R01GM136202 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HANDEL, TRACY M, KUFAREVA, IRINA · 2020 to 2023
$1.9M
Spatiotemporally resolved architecture of G protein signaling downstream of CXCR4, the driver of lymphocyte migrationR21AI156662 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KUFAREVA, IRINA · 2021 to 2022
$434k
NIAID NIH HHS R01 AI161880NIAID NIH HHS R21 AI156662NIGMS NIH HHS R01 GM136202NIGMS NIH HHS R35 GM127121NIGMS NIH HHS T32 GM007198NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

The α-arrestin ARRDC3 is a recently discovered tumor suppressor in invasive breast cancer that functions as a multifaceted adaptor protein to control protein trafficking and cellular signaling. However, the molecular mechanisms that control ARRDC3 function are unknown. Other arrestins are known to be regulated by posttranslational modifications, suggesting that ARRDC3 may be subject to similar regulatory mechanisms. Here we report that ubiquitination is a key regulator of ARRDC3 function and is mediated primarily by two proline-rich PPXY motifs in the ARRDC3 C-tail domain. Ubiquitination and the PPXY motifs are essential for ARRDC3 function in regulating GPCR trafficking and signaling. Additionally, ubiquitination and the PPXY motifs mediate ARRDC3 protein degradation, dictate ARRDC3 subcellular localization, and are required for interaction with the NEDD4-family E3 ubiquitin ligase WWP2. These studies demonstrate a role for ubiquitination in regulating ARRDC3 function and reveal a mechanism by which ARRDC3 divergent functions are controlled.

Indexed as

ArrestinArrestinsNedd4 Ubiquitin Protein LigasesSignal TransductionUbiquitinationUbiquitin-Protein LigasesArrestinArrestinsNedd4 Ubiquitin Protein LigasesUbiquitin-Protein Ligases

Identifiers

PMID37223976
PMCPMC10398895
OpenAlexW4377939788

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.