Evidence map›Paper›PMID 22645313›Full record

ArticleMolecular and cellular biology2012

Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes.

Gustavo Martínez-Noël, Jeffrey T Galligan, Mathew E Sowa, Verena Arndt, Thomas M Overton, J Wade Harper, Peter M Howley

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

72 citing papers in PubMed, 102 citations in OpenAlex.

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  14. Regulation of MAPK Signaling Pathways by the Large HERC Ubiquitin Ligases.International journal of molecular sciences · 2023
    Review
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12 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

7 authors at 1 institution in 1 country.

Gustavo Martínez-NoëlDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA.
Jeffrey T Galligan
Mathew E Sowa
Verena Arndt
Thomas M Overton
J Wade Harper
Peter M Howley
Harvard University · US

Funding

VIRAL ONCOPROTEIN PERTURBATION OF RB/E2F PATHWAYP01CA050661 · NCI · DANA-FARBER CANCER INSTITUTE · PI HOWLEY, PETER M · 1989 to 2013
$35.8M
SYSTEMATIC ANALYSIS OF THE DUB PROTEOMER01GM054137 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HARPER, JEFFREY W · 1996 to 2012
$4.1M
SYSTEMATIC ANALYSIS OF PROTEOLYSIS PATHWAYS FOR CULLIN TARGETSR01GM070565 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HARPER, JEFFREY W · 2005 to 2012
$2.6M
NCI NIH HHS P01 CA050661NCI NIH HHS P01CA50661NIGMS NIH HHS R01 GM054137NIGMS NIH HHS R01GM054137NIGMS NIH HHS R01 GM070565NIGMS NIH HHS R01GM070565
6 · The paper itself

Abstract

The E6AP ubiquitin ligase catalyzes the high-risk human papillomaviruses' E6-mediated ubiquitylation of p53, contributing to the neoplastic progression of cells infected by these viruses. Defects in the activity and the dosage of E6AP are linked to Angelman syndrome and to autism spectrum disorders, respectively, highlighting the need for precise control of the enzyme. With the exception of HERC2, which modulates the ubiquitin ligase activity of E6AP, little is known about the regulation or function of E6AP normally. Using a proteomic approach, we have identified and validated several new E6AP-interacting proteins, including HIF1AN, NEURL4, and mitogen-activated protein kinase 6 (MAPK6). E6AP exists as part of several different protein complexes, including the proteasome and an independent high-molecular-weight complex containing HERC2, NEURL4, and MAPK6. In examining the functional consequence of its interaction with the proteasome, we found that UBE3C (another proteasome-associated ubiquitin ligase), but not E6AP, contributes to proteasomal processivity in mammalian cells. We also found that E6 associates with the HERC2-containing high-molecular-weight complex through its binding to E6AP. These proteomic studies reveal a level of complexity for E6AP that has not been previously appreciated and identify a number of new cellular proteins through which E6AP may be regulated or functioning.

Indexed as

Angelman SyndromeGuanine Nucleotide Exchange FactorsHEK293 CellsHeLa CellsHumansMitogen-Activated Protein Kinase 6Mixed Function OxygenasesPapillomaviridaeProteasome Endopeptidase ComplexProtein BindingProteomicsRepressor ProteinsRNA InterferenceRNA, Small InterferingTumor Suppressor Protein p53UbiquitinationGuanine Nucleotide Exchange FactorsHERC2 protein, humanHIF1AN protein, humanMitogen-Activated Protein Kinase 6Mixed Function OxygenasesProteasome Endopeptidase ComplexRepressor ProteinsRNA, Small InterferingTumor Suppressor Protein p53UBE3A protein, humanUbiquitin-Protein Ligases

Identifiers

PMID22645313
PMCPMC3434508
OpenAlexW2131492461

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.