Evidence map›Paper›PMID 24344129›Full record

ArticleThe Journal of biological chemistry2014

UBE4B protein couples ubiquitination and sorting machineries to enable epidermal growth factor receptor (EGFR) degradation.

Natalie Sirisaengtaksin, Monica Gireud, Qing Yan, Yoshihisa Kubota, Denisse Meza, Jack C Waymire, Peter E Zage, Andrew J Bean

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
  6. The SWIB/MDM2 motif of UBE4B activates the p53 pathway.Molecular therapy. Nucleic acids · 2023
    Article
  7. Article
  8. O-GlcNAcylation regulates epidermal growth factor receptor intracellular trafficking and signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  12. Article
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  15. Review
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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

8 authors at 2 institutions in 1 country.

Natalie SirisaengtaksinFrom the Department of Neurobiology and Anatomy and the Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, Texas 77030.
Monica Gireud
Qing Yan
Yoshihisa Kubota
Denisse Meza
Jack C Waymire
Peter E Zage
Andrew J Bean
The University of Texas Health Science Center at Houston · USBaylor College of Medicine · US

Funding

MOLECULAR MECHANISMS OF NEUROTRANSMITTER SECRETIONR01MH058920 · NIMH · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI BEAN, ANDREW J · 1998 to 2010
$2.9M
The Role of Growth Factor Receptor Trafficking in TumorigenesisR01CA166749 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZAGE, PETER E. · 2013 to 2017
$1.7M
NCI NIH HHS CA166749NCI NIH HHS R01 CA166749NIMH NIH HHS MH58920NIMH NIH HHS R01 MH058920
6 · The paper itself

Abstract

The signaling of plasma membrane proteins is tuned by internalization and sorting in the endocytic pathway prior to recycling or degradation in lysosomes. Ubiquitin modification allows recognition and association of cargo with endosomally associated protein complexes, enabling sorting of proteins to be degraded from those to be recycled. The mechanism that provides coordination between the cellular machineries that mediate ubiquitination and endosomal sorting is unknown. We report that the ubiquitin ligase UBE4B is recruited to endosomes in response to epidermal growth factor receptor (EGFR) activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0. We identify the EGFR as a substrate for UBE4B, establish UBE4B as a regulator of EGFR degradation, and describe a mechanism by which UBE4B regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. We propose a model in which the coordinated action of UBE4B, ESCRT-0, and the deubiquitinating enzyme USP8 enable the endosomal sorting and lysosomal degradation of the EGFR.

Indexed as

Cell MembraneEndopeptidasesEndosomal Sorting Complexes Required for TransportEndosomesErbB ReceptorsHeLa CellsHumansMembrane ProteinsPhosphoproteinsProtein Interaction Domains and MotifsProtein Structure, TertiaryProtein TransportProteolysisSignal TransductionTumor Suppressor ProteinsUbiquitinationEGFR protein, humanEndopeptidasesEndosomal Sorting Complexes Required for TransportErbB Receptorshepatocyte growth factor-regulated tyrosine kinase substrateMembrane ProteinsPhosphoproteinsTumor Suppressor ProteinsUBE4B protein, humanUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbiquitin ThiolesteraseUSP8 protein, humanDeubiquitinationE3 Ubiquitin LigaseEndocytosisEndosomesESCRTProtein SortingUbiquitinationUSP8

Identifiers

PMID24344129
PMCPMC3908433
OpenAlexW2034173685

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.