Evidence map›Paper›PMID 26744419›Full record

ArticleGenes & development2016

Control of heterochromatin localization and silencing by the nuclear membrane protein Lem2.

Ramón Ramos Barrales, Marta Forn, Paula Raluca Georgescu, Zsuzsa Sarkadi, Sigurd Braun

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing 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

78 citing papers in PubMed, 127 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Fungi as models of centromere innovation: from DNA sequence to 3-dimensional arrangement.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Ramón Ramos BarralesDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany;
Marta FornDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany;
Paula Raluca GeorgescuDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany;
Zsuzsa SarkadiDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany;
Sigurd BraunDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, 82152 Martinsried, Germany; International Max Planck Research School for Molecular and Cellular Life Sciences, 82152 Martinsried, Germany.
Ludwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcriptionally silent chromatin localizes to the nuclear periphery, which provides a special microenvironment for gene repression. A variety of nuclear membrane proteins interact with repressed chromatin, yet the functional role of these interactions remains poorly understood. Here, we show that, in Schizosaccharomyces pombe, the nuclear membrane protein Lem2 associates with chromatin and mediates silencing and heterochromatin localization. Unexpectedly, we found that these functions can be separated and assigned to different structural domains within Lem2, excluding a simple tethering mechanism. Chromatin association and tethering of centromeres to the periphery are mediated by the N-terminal LEM (LAP2-Emerin-MAN1) domain of Lem2, whereas telomere anchoring and heterochromatin silencing require exclusively its conserved C-terminal MSC (MAN1-Src1 C-terminal) domain. Particularly, silencing by Lem2 is epistatic with the Snf2/HDAC (histone deacetylase) repressor complex SHREC at telomeres, while its necessity can be bypassed by deleting Epe1, a JmjC protein with anti-silencing activity. Furthermore, we found that loss of Lem2 reduces heterochromatin association of SHREC, which is accompanied by increased binding of Epe1. This reveals a critical function of Lem2 in coordinating these antagonistic factors at heterochromatin. The distinct silencing and localization functions mediated by Lem2 suggest that these conserved LEM-containing proteins go beyond simple tethering to play active roles in perinuclear silencing.

Indexed as

Gene DeletionGene SilencingHeterochromatinNuclear ProteinsProtein BindingProtein Structure, TertiaryProtein TransportSchizosaccharomycesSchizosaccharomyces pombe Proteinsepe1 protein, S pombeHeterochromatinNuclear ProteinsSchizosaccharomyces pombe Proteinsheterochromatinlamin-associated proteinsLEMnuclear peripheryperinuclear silencingtethering

Identifiers

PMID26744419
PMCPMC4719305
OpenAlexW2228899249

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.