Evidence map›Paper›PMID 26391951›Full record

ArticleMolecular and cellular biology2015

Independent Mechanisms Target SMCHD1 to Trimethylated Histone H3 Lysine 9-Modified Chromatin and the Inactive X Chromosome.

Nicholas J Brideau, Heather Coker, Anne-Valerie Gendrel, C Alistair Siebert, Karel Bezstarosti, Jeroen Demmers, Raymond A Poot, Tatyana B Nesterova, Neil Brockdorff

Open access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed, 80 citations in OpenAlex.

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  19. Adenine base editing of theMolecular therapy. Nucleic acids · 2021
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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

9 authors at 2 institutions in 2 countries.

Nicholas J BrideauDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Heather CokerDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Anne-Valerie GendrelDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
C Alistair SiebertOxford Particle Imaging Centre, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Karel BezstarostiProteomics Center, Erasmus MC, Rotterdam, The Netherlands.
Jeroen DemmersProteomics Center, Erasmus MC, Rotterdam, The Netherlands.
Raymond A PootDepartment of Cell Biology, Erasmus MC, Rotterdam, The Netherlands.
Tatyana B NesterovaDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Neil BrockdorffDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom neil.brockdorff@bioch.ox.ac.uk.
University of Oxford · GBErasmus University Rotterdam · NL

Funding

Wellcome Trust 060208/Z/00/ZWellcome Trust 081385Wellcome Trust 093305/Z/10/ZWellcome Trust 103768
6 · The paper itself

Abstract

The chromosomal protein SMCHD1 plays an important role in epigenetic silencing at diverse loci, including the inactive X chromosome, imprinted genes, and the facioscapulohumeral muscular dystrophy locus. Although homology with canonical SMC family proteins suggests a role in chromosome organization, the mechanisms underlying SMCHD1 function and target site selection remain poorly understood. Here we show that SMCHD1 forms an active GHKL-ATPase homodimer, contrasting with canonical SMC complexes, which exist as tripartite ring structures. Electron microscopy analysis demonstrates that SMCHD1 homodimers structurally resemble prokaryotic condensins. We further show that the principal mechanism for chromatin loading of SMCHD1 involves an LRIF1-mediated interaction with HP1γ at trimethylated histone H3 lysine 9 (H3K9me3)-modified chromatin sites on the chromosome arms. A parallel pathway accounts for chromatin loading at a minority of sites, notably the inactive X chromosome. Together, our results provide key insights into SMCHD1 function and target site selection.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsCell LineChromatinChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHEK293 CellsHistonesHumansLysineMiceModels, MolecularMolecular Sequence DataProtein Interaction MapsProtein MultimerizationAdenosine TriphosphatasesChromatinChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHistonesLysineSMCHD1 protein, humanSmcHD1 protein, mouse

Identifiers

PMID26391951
PMCPMC4628070
OpenAlexW2172454326

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.