Evidence map›Paper›PMID 25128498›Full record

ArticleGenes & development2014

The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.

Gary M R Deyter, Sue Biggins

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed, 74 citations in OpenAlex.

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  20. Epigenetic regulation of centromere function.Cellular and molecular life sciences : CMLS · 2020
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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

2 authors at 1 institution in 1 country.

Gary M R DeyterDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.
Sue BigginsDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA sbiggins@fhcrc.org.
Fred Hutch Cancer Center · US

Funding

Translational Bioimaging Core Shared ResourceP30CA015704 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Marian Esvelt · 1985 to 2026
$296.4M
Regulation of Centromeric ChromatinR01GM078069 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BIGGINS, SUSAN · 2007 to 2015
$2.7M
NCI NIH HHS P30 CA015704NIGMS NIH HHS GM078069NIGMS NIH HHS R01 GM078069
6 · The paper itself

Abstract

Centromere identity and its epigenetic maintenance require the incorporation of a histone H3 variant called CENP-A at centromeres. CENP-A mislocalization to ectopic sites may disrupt chromatin-based processes and chromosome segregation, so it is important to uncover the mechanisms by which this variant is exclusively localized to centromeres. Here, we identify a role for the conserved chromatin-modifying complex FACT (facilitates chromatin transcription/transactions) in preventing budding yeast CENP-A(Cse4) mislocalization to euchromatin by mediating its proteolysis. The Spt16 subunit of the FACT complex binds to Psh1 (Pob3/Spt16/histone), an E3 ubiquitin ligase that targets CENP-A(Cse4) for degradation. The interaction between Psh1 and Spt16 is critical for both CENP-A(Cse4) ubiquitylation and its exclusion from euchromatin. We found that Psh1 cannot efficiently ubiquitylate CENP-A(Cse4) nucleosomes in vitro, suggesting that additional factors must facilitate CENP-A(Cse4) removal from chromatin in vivo. Consistent with this, a Psh1 mutant that cannot associate with FACT has a reduced interaction with CENP-A(Cse4) in vivo. Together, our data identify a previously unknown mechanism to maintain centromere identity and genomic stability through the FACT-mediated degradation of ectopically localized CENP-A(Cse4).

Indexed as

AutoantigensCentromere Protein AChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEuchromatinHigh Mobility Group ProteinsMutationNucleosomesPeptide Elongation FactorsProtein BindingProtein StabilityProtein TransportProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsAutoantigensCentromere Protein AChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEuchromatinFACT protein, S cerevisiaeHigh Mobility Group ProteinsNucleosomesPeptide Elongation FactorsPsh1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT16 protein, S cerevisiaeTranscriptional Elongation FactorsUbiquitin-Protein LigasesCENP-AcentromereFACTproteolysisPsh1ubiquitylation

Identifiers

PMID25128498
PMCPMC4197964
OpenAlexW2103111663

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.