Evidence map›Paper›PMID 20797632›Full record

ArticleMolecular cell2010

A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.

Belinda J Westman, Céline Verheggen, Saskia Hutten, Yun Wah Lam, Edouard Bertrand, Angus I Lamond

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

51 citing papers in PubMed, 82 citations in OpenAlex.

  1. Intronic polyadenylation-derived long noncoding RNA modulates nucleolar integrity and function.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  12. The roles of NOP56 in cancer and SCA36.Pathology oncology research : POR · 2023
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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

6 authors at 4 institutions in 3 countries.

Belinda J WestmanWellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD15EH, UK.
Céline Verheggen
Saskia Hutten
Yun Wah Lam
Edouard Bertrand
Angus I Lamond
Centre National de la Recherche Scientifique · FRUniversity of Dundee · GBCity University of Hong Kong · HKWellcome Trust · GB

Funding

Medical Research Council 69159Medical Research Council G0301131Wellcome Trust 073980Wellcome Trust 083524/Z/07/Z
6 · The paper itself

Abstract

Posttranslational SUMO modification is an important mechanism of regulating protein function, especially in the cell nucleus. The nucleolus is the subnuclear organelle responsible for rRNA synthesis, processing, and assembly of the large and small ribosome subunits. Here, we have used SILAC-based quantitative proteomics to identify nucleolar SUMOylated proteins. This reveals a role for SUMOylation in the biogenesis and/or function of small nucleolar ribonucleoprotein complexes (snoRNPs) via the targeting of Nhp2 and Nop58. Using combined in vitro and in vivo approaches, both Nhp2 and Nop58 (also known as Nop5) are shown to be substrates for SUMOylation. Mutational analyses revealed the sites of modification on Nhp2 as K5, and on Nop58 as K467 and K497. Unlike Nop58 and Nhp2, the closely related Nop56 and 15.5K proteins appear not to be SUMO targets. SUMOylation is essential for high-affinity Nop58 binding to snoRNAs. This study provides direct evidence linking SUMO modification with snoRNP function.

Indexed as

Protein Processing, Post-TranslationalProteomicsAmino Acid SequenceAnimalsBinding SitesCell NucleolusChromosomal Proteins, Non-HistoneHeLa CellsHumansLysineMolecular Sequence DataMutationNuclear ProteinsRatsRecombinant Fusion ProteinsRibonucleoproteins, Small NuclearChromosomal Proteins, Non-HistonefibrillarinLysineNHP2 protein, humanNOP56 protein, humanNOP58 protein, humanNuclear ProteinsRecombinant Fusion ProteinsRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarSmall Ubiquitin-Related Modifier ProteinsSnu13 protein, humanSUMO-1 ProteinSUMO1 protein, humanSUMO2 protein, humanSUMO3 protein, humanUbiquitins

Identifiers

PMID20797632
PMCPMC2938476
OpenAlexW1977792673

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.