Evidence map›Paper›PMID 28487408›Full record

ArticleGenes & development2017

Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity.

Jason Liang, Namit Singh, Christopher R Carlson, Claudio P Albuquerque, Kevin D Corbett, Huilin Zhou

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed, 38 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 2 countries.

Jason LiangLudwig Institute for Cancer Research, San Diego Branch, La Jolla, California 92093, USA.ORCID 0000-0002-7041-9136
Namit SinghLudwig Institute for Cancer Research, San Diego Branch, La Jolla, California 92093, USA.
Christopher R CarlsonLudwig Institute for Cancer Research, San Diego Branch, La Jolla, California 92093, USA.
Claudio P AlbuquerqueLudwig Institute for Cancer Research, San Diego Branch, La Jolla, California 92093, USA.
Kevin D CorbettLudwig Institute for Cancer Research, San Diego Branch, La Jolla, California 92093, USA.
Huilin ZhouLudwig Institute for Cancer Research, San Diego Branch, La Jolla, California 92093, USA.
Ludwig Cancer Research · BE

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Contemporary Approaches to Cancer Cell Signaling and CommunicationT32CA009523 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DONOGHUE, DANIEL J, YANG, JING · 1985 to 2025
$12.1M
Molecular mechanisms of chromosome organization and recombination control by the meiotic chromosome axis.R01GM104141 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CORBETT, KEVIN DANIEL · 2013 to 2021
$3.1M
Suppression of duplication-mediated genome rearrangements by protein sumoylationR01GM116897 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHOU, HUILIN · 2015 to 2023
$2.6M
Regulation of Receptor Tyrosine KinasesR01GM065490 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI DONOGHUE, DANIEL J · 2002 to 2005
$1.0M
NCI NIH HHS T32 CA009523NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM065490NIGMS NIH HHS R01 GM104141NIGMS NIH HHS R01 GM116897
6 · The paper itself

Abstract

Post-translational modification by SUMO (small ubiquitin-like modifier) plays important but still poorly understood regulatory roles in eukaryotic cells, including as a signal for ubiquitination by SUMO targeted ubiquitin ligases (STUbLs). Here, we delineate the molecular mechanisms for SUMO-dependent control of ribosomal DNA (rDNA) silencing through the opposing actions of a STUbL (Slx5:Slx8) and a SUMO isopeptidase (Ulp2). We identify a conserved region in the Ulp2 C terminus that mediates its specificity for rDNA-associated proteins and show that this region binds directly to the rDNA-associated protein Csm1. Two crystal structures show that Csm1 interacts with Ulp2 and one of its substrates, the rDNA silencing protein Tof2, through adjacent conserved interfaces in its C-terminal domain. Disrupting Csm1's interaction with either Ulp2 or Tof2 dramatically reduces rDNA silencing and causes a marked drop in Tof2 abundance, suggesting that Ulp2 promotes rDNA silencing by opposing STUbL-mediated degradation of silencing proteins. Tof2 abundance is rescued by deletion of the STUbL

Indexed as

Gene SilencingModels, MolecularAmino Acid MotifsCell Cycle ProteinsCell NucleolusCrystallizationDNA, RibosomalEndopeptidasesIntracellular Signaling Peptides and ProteinsNuclear ProteinsProtein BindingProtein StabilityProtein Structure, QuaternaryProteolysisSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsCell Cycle ProteinsCSM1 protein, S cerevisiaeDNA, RibosomalEndopeptidasesIntracellular Signaling Peptides and ProteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsSlx5 protein, S cerevisiaeSlx8 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsTOF2 protein, S cerevisiaeUbiquitin-Protein LigasesULP2 protein, S cerevisiaecohibindesumoylationmonopolinrDNA silencingRENT complexSTUbLsumoylation

Identifiers

PMID28487408
PMCPMC5435892
OpenAlexW2612612834

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.