Evidence map›Paper›PMID 10938122›Full record

ArticleMolecular and cellular biology2000

Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: direct chromoshadow domain-KAP-1 corepressor interaction is essential.

M S Lechner, G E Begg, D W Speicher, F J Rauscher

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

103 citing papers in PubMed, 208 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. KAP1 in antiviral immunity: dual roles in viral silencing and immune regulation.Frontiers in cellular and infection microbiology · 2025
    Review
  7. Article
  8. Article
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  11. Review
  12. Article
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  16. Review
  17. Article
  18. Article
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43 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

4 authors at 1 institution in 1 country.

M S LechnerThe Wistar Institute, Philadelphia, Pennsylvania 19104, USA.
G E Begg
D W Speicher
F J Rauscher
The Wistar Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
ZINC FINGER PROTEINS IN EARLY KIDNEY DEVELOPMENTP01DK049210 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI AHIMA, REXFORD S. · 1995 to 2016
$26.9M
TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
STRUCTURE/FUNCTION OF THE CO17-1A/GA733 ANTIGENP01CA074294 · NCI · WISTAR INSTITUTE · PI HERLYN, DOROTHEE M · 1998 to 2002
$3.9M
STRUCTURE FUNCTION OF MELCAM, A CELL ADHESION PROTEINR01CA066671 · NCI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 1996 to 2000
$319k
NCI NIH HHS CA 09171NCI NIH HHS CA 66671NCI NIH HHS CA 74294NCI NIH HHS P01 CA074294NCI NIH HHS P30 CA010815NCI NIH HHS T32 CA009171NIDDK NIH HHS P01 DK049210
6 · The paper itself

Abstract

The KRAB domain is a highly conserved transcription repression module commonly found in eukaryotic zinc finger proteins. KRAB-mediated repression requires binding to the KAP-1 corepressor, which in turn recruits members of the heterochromatin protein 1 (HP1) family. The HP1 proteins are nonhistone chromosomal proteins, although it is unclear how they are targeted to unique chromosomal domains or promoters. In this report, we have reconstituted and characterized the HP1-KAP-1 interaction using purified proteins and have compared KAP-1 to three other known HP1 binding proteins: SP100, lamin B receptor (LBR), and the p150 subunit from chromatin assembly factor (CAF-1 p150). We show that the chromoshadow domain (CSD) of HP1 is a potent repression domain that binds directly to all four previously described proteins. For KAP-1, we have mapped the CSD interaction region to a 15-amino-acid segment, termed the HP1BD, which is also present in CAF-1 p150 but not SP100 or LBR. The region of KAP-1 harboring the HP1BD binds as a monomer to a dimer of the CSD, as revealed by gel filtration, analytical ultracentrifugation, and optical biosensor analyses. The use of a spectrum of amino acid substitutions in the human HP1alpha CSD revealed a strong correlation between CSD-mediated repression and binding to KAP-1, CAF-1 p150, and SP100 but not LBR. Differences among the HP1 binding partners could also be discerned by fusion to a heterologous DNA binding domain and by the potential to act as dominant negative molecules. Together, these results strongly suggest that KAP-1 is a physiologically relevant target for HP1 function.

Indexed as

Antigens, NuclearTranscription Factors3T3 CellsAmino Acid SequenceAnimalsAutoantigensChromatin Assembly Factor-1Chromatography, GelChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA Mutational AnalysisGene SilencingGlutathione TransferaseHumansKineticsAntigens, NuclearAutoantigensCBX5 protein, humanChaf1a protein, mouseCHAF1B protein, humanChromatin Assembly Factor-1Chromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneCNOT8 protein, humanDNA-Binding ProteinsGlutathione TransferaseNuclear ProteinsRecombinant Fusion ProteinsRepressor ProteinsSP100 protein, humanTranscription FactorsTRIM28 protein, humanTrim28 protein, mouseTripartite Motif-Containing Protein 28

Identifiers

PMID10938122
PMCPMC86120
OpenAlexW2129274682

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.