Evidence map›Paper›PMID 19567367›Full record

ArticleMolecular & cellular proteomics : MCP2009

Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications.

Gary LeRoy, John T Weston, Barry M Zee, Nicolas L Young, Mariana D Plazas-Mayorca, Benjamin A Garcia

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.2field-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

64 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Review
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  4. Multimodal interactions drive chromatin phase separation and compaction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Epigenetic meets metabolism: novel vulnerabilities to fight cancer.Cell communication and signaling : CCS · 2023
    Review
  6. HP1-driven phase separation recapitulates the thermodynamics and kinetics of heterochromatin condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Review
  9. Article
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  11. Review
  12. Review
  13. Article
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4 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Gary LeRoyDepartment Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
John T Weston
Barry M Zee
Nicolas L Young
Mariana D Plazas-Mayorca
Benjamin A Garcia
Princeton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterochromatin protein 1 (HP1) family members (alpha, beta, and gamma) bind histone H3 methylated at Lys-9, leading to gene silencing and heterochromatin formation. Several previous reports have suggested that HP1s are post-translationally modified, yet sites of modification have not yet been exhaustively determined. Here we perform the first comprehensive proteomic analysis of all HP1 isoforms using tandem mass spectrometry. Our data reveal that all HP1 isoforms are highly modified in a manner analogous to histones including phosphorylation, acetylation, methylation, and formylation, including several sites having multiple different types of modifications. Additionally, many of these modifications are found in both the chromo- and chromoshadow domains, suggesting that they may have an important role in modulating HP1 interactions or functions. These studies are the first to systematically map the abundant sites of covalent modifications on HP1 isoforms and provide the foundation for future investigations to test whether these modifications are essential in heterochromatin maintenance or other nuclear processes.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCell NucleusChromatography, LiquidChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDrosophilaHistonesHumansMass SpectrometryMolecular Sequence DataPeptidesProtein IsoformsProteomicsTandem Mass SpectrometryChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHistonesPeptidesProtein Isoforms

Identifiers

PMID19567367
PMCPMC2773712
OpenAlexW2166723971

What OpenQuestion holds

Textmetadata
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.