Evidence map›Paper›PMID 12186903›Full record

ArticleJournal of virology2002

Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery.

Josephine N Harada, Anna Shevchenko, Andrej Shevchenko, David C Pallas, Arnold J Berk

Abstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

134 citing papers in PubMed, 220 citations in OpenAlex.

  1. Article
  2. Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023
    Review
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74 more citing papers are in PubMed but not listed here.

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

5 authors at 4 institutions in 4 countries.

Josephine N HaradaMolecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90095-1570, USA.
Anna Shevchenko
Andrej Shevchenko
David C Pallas
Arnold J Berk
Emory University · USInstitute of Molecular Biology · BGMax Planck Institute of Molecular Cell Biology and Genetics · DEUniversity of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
ROLE OF PP2A IN POLYOMAVIRUS TUMOR ANTIGEN FUNCTIONSR01CA057327 · NCI · EMORY UNIVERSITY · PI PALLAS, DAVID C · 1992 to 2012
$4.1M
MECHANISM OF P53 SILENCING BY ADENOVIRUS E2B 55K PROTEINR01CA064799 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BERK, ARNOLD J · 1995 to 2011
$2.1M
NCI NIH HHS CA57327NCI NIH HHS CA 64799NCI NIH HHS R01 CA057327NCI NIH HHS R01 CA064799NIGMS NIH HHS GM07185NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

During the early phase of infection, the E1B-55K protein of adenovirus type 5 (Ad5) counters the E1A-induced stabilization of p53, whereas in the late phase, E1B-55K modulates the preferential nucleocytoplasmic transport and translation of the late viral mRNAs. The mechanism(s) by which E1B-55K performs these functions has not yet been clearly elucidated. In this study, we have taken a proteomics-based approach to identify and characterize novel E1B-55K-associated proteins. A multiprotein E1B-55K-containing complex was immunopurified from Ad5-infected HeLa cells and found to contain E4-orf6, as well as several cellular factors previously implicated in the ubiquitin-proteasome-mediated destruction of proteins, including Cullin-5, Rbx1/ROC1/Hrt1, and Elongins B and C. We further demonstrate that a complex containing these as well as other proteins is capable of directing the polyubiquitination of p53 in vitro. These ubiquitin ligase components were found in a high-molecular-mass complex of 800 to 900 kDa. We propose that these newly identified binding partners (Cullin-5, Elongins B and C, and Rbx1) complex with E1B-55K and E4-orf6 during Ad infection to form part of an E3 ubiquitin ligase that targets specific protein substrates for degradation. We further suggest that E1B-55K functions as the principal substrate recognition component of this SCF-type ubiquitin ligase, whereas E4-orf6 may serve to nucleate the assembly of the complex. Lastly, we describe the identification and characterization of two novel E1B-55K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previously ascribed to E1B-55K and E4-orf6.

Indexed as

ProteomeAdenovirus E1B ProteinsAdenovirus E4 ProteinsAdenoviruses, HumanCell LineCell NucleusCysteine EndopeptidasesHeLa CellsHumansLigasesMultienzyme ComplexesPrecipitin TestsProteasome Endopeptidase ComplexSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTransfectionTumor Suppressor Protein p53Adenovirus E1B ProteinsAdenovirus E4 ProteinsCysteine EndopeptidasesLigasesMultienzyme ComplexesProteasome Endopeptidase ComplexProteomeTumor Suppressor Protein p53UbiquitinUbiquitin-Protein LigasesViral Proteins

Identifiers

PMID12186903
PMCPMC136464
OpenAlexW2166002553

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.