Evidence map›Paper›PMID 20357094›Full record

ArticleJournal of virology2010

p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha.

Christopher O'Connor, Thomas Pertel, Seth Gray, Seth L Robia, Joanna C Bakowska, Jeremy Luban, Edward M Campbell

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.4field-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

42 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019
    Review
  16. Article
  17. Article
  18. PB1 and UBA domains of p62 are essential for aggresome-like induced structure formation.Biochemical and biophysical research communications · 2018
    Article
  19. Article
  20. Review
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

7 authors at 2 institutions in 2 countries.

Christopher O'ConnorDepartment of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois, USA.
Thomas Pertel
Seth Gray
Seth L Robia
Joanna C Bakowska
Jeremy Luban
Edward M Campbell
Loyola University Chicago · USUniversity of Geneva · CH

Funding

Cyclophilin A Function in the Immune SystemR01AI059159 · NIAID · UNIVERSITY OF GENEVA · PI LUBAN, JEREMY · 2006 to 2011
$1.4M
Analysis of restriction factor function in situK22AI078757 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI CAMPBELL, EDWARD M · 2009 to 2010
$270k
NIAID NIH HHS K22 AI078757NIAID NIH HHS R01 AI059159NIAID NIH HHS R01AI59159
6 · The paper itself

Abstract

TRIM5 proteins mediate a potent block to the cross-species transmission of retroviruses, the most well known being the TRIM5alpha protein from rhesus macaques, which potently inhibits human immunodeficiency virus type 1 (HIV-1) infection. This restriction occurs at an early stage in the replication cycle and is mediated by the binding of TRIM5 proteins to determinants present in the retroviral capsid. TRIM5alpha, as well as other TRIM family proteins, has been shown to be regulated by interferons (IFN). Here we show that TRIM5alpha associates with another IFN-induced gene, sequestosome-1/p62 (p62). p62 plays a role in several signal transduction cascades that are important for maintaining the antiviral state of cells. Here we demonstrate that p62 localizes to both human and rhesus macaque TRIM5alpha cytoplasmic bodies, and fluorescence resonance energy transfer (FRET) analysis demonstrates that these proteins closely associate in these structures. When p62 expression was knocked down via small interfering RNA (siRNA), the number of TRIM5alpha cytoplasmic bodies and the level of TRIM5alpha protein expression were reduced in cell lines stably expressing epitope-tagged versions of TRIM5alpha. In accordance with these data, p62 knockdown resulted in reduced TRIM5alpha-mediated retroviral restriction in cells expressing epitope-tagged TRIM5alpha or expressing endogenously expressed human TRIM5alpha. p62 may therefore operate to enhance TRIM5alpha-mediated retroviral restriction, contributing to the antiviral state of cells following IFN treatment.

Indexed as

Adaptor Proteins, Signal TransducingAntiviral Restriction FactorsCarrier ProteinsCell LineHIV-1HIV InfectionsHumansProtein BindingRetroviridaeRetroviridae InfectionsSequestosome-1 ProteinTripartite Motif ProteinsUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingAntiviral Restriction FactorsCarrier ProteinsSequestosome-1 ProteinSQSTM1 protein, humanTRIM5 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID20357094
PMCPMC2876647
OpenAlexW2096831872

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.