Evidence map›Paper›PMID 20233849›Full record

ArticleJournal of cell science2010

N4BP1 is a newly identified nucleolar protein that undergoes SUMO-regulated polyubiquitylation and proteasomal turnover at promyelocytic leukemia nuclear bodies.

Prashant Sharma, Rodolfo Murillas, Huafeng Zhang, Michael R Kuehn

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

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  14. Fanconi anemia protein FANCI functions in ribosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

4 authors at 3 institutions in 2 countries.

Prashant SharmaLaboratory of Protein Dynamics and Signaling, Center for Cancer Research, National Cancer Institute, NCI-Frederick, Frederick, MD 21702, USA.
Rodolfo Murillas
Huafeng Zhang
Michael R Kuehn
National Cancer Institute · USCenter for Cancer Research · USCentre for Biomedical Network Research on Rare Diseases · ES

Funding

Ubiquitin And SUMO Post-Translational Modifications In Development And DiseaseZIABC009297 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KUEHN, MICHAEL · 2009 to 2013
$2.8M
6 · The paper itself

Abstract

A number of proteins can be conjugated with both ubiquitin and the small ubiquitin-related modifier (SUMO), with crosstalk between these two post-translational modifications serving to regulate protein function and stability. We previously identified N4BP1 as a substrate for monoubiquitylation by the E3 ubiquitin ligase Nedd4. Here, we describe Nedd4-mediated polyubiquitylation and proteasomal degradation of N4BP1. In addition, we show that N4BP1 can be conjugated with SUMO1 and that this abrogates N4BP1 ubiquitylation. Consistent with this, endogenous N4BP1 is stabilized in primary embryonic fibroblasts from mutants of the desumoylating enzyme SENP1, which show increased steady-state sumoylation levels. We have localized endogenous N4BP1 predominantly to the nucleolus in primary cells. However, a small fraction is found at promyelocytic leukemia (PML) nuclear bodies (NBs). In cells deficient for SENP1 or in wild-type cells treated with the proteasome inhibitor MG132, there is considerable accumulation of N4BP1 at PML NBs. These findings suggest a dynamic interaction between subnuclear compartments, and a role for post-translational modification by ubiquitin and SUMO in the regulation of nucleolar protein turnover.

Indexed as

AnimalsCarrier ProteinsCell LineCell NucleolusCysteine EndopeptidasesEmbryo, MammalianEndopeptidasesIntranuclear Inclusion BodiesLeukemia, Promyelocytic, AcuteMiceModels, BiologicalMutationNuclear ProteinsPolyubiquitinProteasome Endopeptidase ComplexProteasome InhibitorsCarrier ProteinsCysteine EndopeptidasesEndopeptidasesN4BP1 protein, mouseNuclear ProteinsPolyubiquitinProteasome Endopeptidase ComplexProteasome InhibitorsSenp1 protein, mouseSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID20233849
PMCPMC2848111
OpenAlexW2138347473

What OpenQuestion holds

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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.