Evidence map›Paper›PMID 24855649›Full record

ArticleThe Journal of biological chemistry2014

Degradation of the deubiquitinating enzyme USP33 is mediated by p97 and the ubiquitin ligase HERC2.

Nickie C Chan, Willem den Besten, Michael J Sweredoski, Sonja Hess, Raymond J Deshaies, David C Chan

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

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  16. G-Protein Dependent Signal Transduction and Ubiquitination in Dictyostelium.International journal of molecular sciences · 2017
    Review
  17. Article
  18. p97/VCP promotes degradation of CRBN substrate glutamine synthetase and neosubstrates.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

6 authors at 2 institutions in 1 country.

Nickie C ChanFrom the Division of Biology and Biological Engineering, the Howard Hughes Medical Institute, and.
Willem den BestenFrom the Division of Biology and Biological Engineering.
Michael J SweredoskiFrom the Division of Biology and Biological Engineering, the Proteome Exploration Laboratory/Beckman Institute, California Institute of Technology, Pasadena, California 91125.
Sonja HessFrom the Division of Biology and Biological Engineering, the Proteome Exploration Laboratory/Beckman Institute, California Institute of Technology, Pasadena, California 91125.
Raymond J DeshaiesFrom the Division of Biology and Biological Engineering, the Howard Hughes Medical Institute, and.
David C ChanFrom the Division of Biology and Biological Engineering, the Howard Hughes Medical Institute, and dchan@caltech.edu.
California Institute of Technology · USHoward Hughes Medical Institute · US

Funding

Mitochondrial Fusion: Analysis of Fzo FunctionR01GM062967 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CHAN, DAVID C · 2001 to 2014
$3.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM062967
6 · The paper itself

Abstract

Because the deubiquitinating enzyme USP33 is involved in several important cellular processes (β-adrenergic receptor recycling, centrosome amplification, RalB signaling, and cancer cell migration), its levels must be carefully regulated. Using quantitative mass spectrometry, we found that the intracellular level of USP33 is highly sensitive to the activity of p97. Knockdown or chemical inhibition of p97 causes robust accumulation of USP33 due to inhibition of its degradation. The p97 adaptor complex involved in this function is the Ufd1-Npl4 heterodimer. Furthermore, we identified HERC2, a HECT domain-containing E3 ligase, as being responsible for polyubiquitination of USP33. Inhibition of p97 causes accumulation of polyubiquitinated USP33, suggesting that p97 is required for postubiquitination processing. Thus, our study has identified several key molecules that control USP33 degradation within the ubiquitin-proteasome system.

Indexed as

ProteolysisAdenosine TriphosphatasesAnimalsCell Cycle ProteinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansMiceNIH 3T3 CellsProteasome Endopeptidase ComplexUbiquitinUbiquitinationUbiquitin-Protein LigasesUbiquitin ThiolesteraseValosin Containing ProteinAdenosine TriphosphatasesCell Cycle ProteinsGuanine Nucleotide Exchange FactorsHERC2 protein, humanHerc2 protein, mouseProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesUbiquitin ThiolesteraseUSP33 protein, humanValosin Containing ProteinDeubiquitinationE3 Ubiquitin LigaseHERC2p97ProteasomeProtein DegradationUbiquitinationUSP33

Identifiers

PMID24855649
PMCPMC4094088
OpenAlexW2005737394

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.