Evidence map›Paper›PMID 26265139›Full record

ArticleBiochemical pharmacology2015

UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP.

Yanfen Teng, Khosrow Rezvani, Mariella De Biasi

Open access · greenAbstract read
In one paragraph

Article in Biochemical pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Nicotinic receptors in airway disease.American journal of physiology. Lung cellular and molecular physiology · 2024
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer.International journal of molecular sciences · 2016
    Review
  12. Article
  13. Review
  14. 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

3 authors at 2 institutions in 1 country.

Yanfen TengDepartment of Neuroscience, Baylor College of Medicine, Houston, TX 77030, United States.
Khosrow RezvaniDivision of Basic Biomedical Sciences, Sanford School of Medicine, The University of South Dakota, Vermillion, SD 57069, United States.
Mariella De BiasiDepartment of Neuroscience, Baylor College of Medicine, Houston, TX 77030, United States; Department of Psychiatry, 415 Curie Blvd., Clinical Research Building 219, Perelman School of Medicine, University of Pennsylvania, Philadelphia, United States. Electronic address: marielde@upenn.edu.
Baylor College of Medicine · USUniversity of South Dakota · US

Funding

Stress, Anxiety, and Nicotine WithdrawalR01DA017173 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI DE BIASI, MARIELLA · 2003 to 2010
$2.2M
Regulation of Proteasomal Function by NicotineR21DA024385 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI DE BIASI, MARIELLA · 2008 to 2009
$307k
NIDA NIH HHS DA017173NIDA NIH HHS DA024385NIDA NIH HHS R01 DA017173NIDA NIH HHS R21 DA024385
6 · The paper itself

Abstract

Neuronal nicotinic acetylcholine receptors (nAChRs) containing the α3 subunit are known for their prominent role in normal ganglionic transmission while their involvement in the mechanisms underlying nicotine addiction and smoking-related disease has been emerging only in recent years. The amount of information available on the maturation and trafficking of α3-containing nAChRs is limited. We previously showed that UBXN2A is a p97 adaptor protein that facilitates the maturation and trafficking of α3-containing nAChRs. Further investigation of the mechanisms of UBXN2A actions revealed that the protein interacts with CHIP (carboxyl terminus of Hsc70 interacting protein), whose ubiquitin E3 ligase activity regulates the degradation of several disease-related proteins. We show that CHIP displays E3 ligase activity toward the α3 nAChR subunit and contributes to its ubiquitination and subsequent degradation. UBXN2A interferes with CHIP-mediated ubiquitination of α3 and protects the nicotinic receptor subunit from endoplasmic reticulum associated degradation (ERAD). UBXN2A also cross-talks with VCP/p97 and HSC70/HSP70 proteins in a complex where α3 is likely to be targeted by CHIP. Overall,we identify CHIP as an E3 ligase for α3 and UBXN2A as a protein that may efficiently regulate the stability of CHIP's client substrates.

Indexed as

AnimalsEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationGene Expression Regulation, EnzymologicGolgi ApparatusHEK293 CellsHumansMaleMiceMice, Inbred C57BLNeuronsNuclear ProteinsPC12 CellsProteasome Endopeptidase ComplexRatsReceptors, Nicotinicnuclear protein import factor p97Nuclear ProteinsProteasome Endopeptidase ComplexReceptors, NicotinicUbiquitin-Protein LigasesCHIPp97Proteasomal degradationUBX domainUBXN2Aα3 Nicotinic subunit

Identifiers

PMID26265139
PMCPMC7780642
OpenAlexW1509002146

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.