Evidence map›Paper›PMID 21865325›Full record

ArticleGenes & development2011

A role for heterochromatin protein 1γ at human telomeres.

Silvia Canudas, Benjamin R Houghtaling, Monica Bhanot, Ghadir Sasa, Sharon A Savage, Alison A Bertuch, Susan Smith

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
–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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 citations in OpenAlex.

  1. Pooled it
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  18. Emerging roles of telomeric chromatin alterations in cancer.Journal of experimental & clinical cancer research : CR · 2019
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12 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

7 authors at 3 institutions in 1 country.

Silvia CanudasMolecular Pathogenesis Program, Department of Pathology, Kimmel Center for Biology and Medicine of the Skirball Institute, New York University School of Medicine, New York, New York 10016, USA.
Benjamin R Houghtaling
Monica Bhanot
Ghadir Sasa
Sharon A Savage
Alison A Bertuch
Susan Smith
New York University · USBaylor College of Medicine · USNational Cancer Institute · US

Funding

Genetic Epidemiology of Telomere Maintenance and Cancer EtiologyZIACP010190 · NCI · DIVISION OF CANCER EPIDEMIOLOGY AND GENETICS · PI SAVAGE, SHARON A. · 2009 to 2025
$10.2M
Mechanisms of Sister Telomere Cohesion and ResolutionR01CA116352 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SMITH, SUSAN · 2007 to 2016
$3.1M
Intramural NIH HHSNCI NIH HHS N02 CP011019NCI NIH HHS N02 CP065501NCI NIH HHS N02 CP065504NCI NIH HHS R01 CA116352
6 · The paper itself

Abstract

Human telomere function is mediated by shelterin, a six-subunit complex that is required for telomere replication, protection, and cohesion. TIN2, the central component of shelterin, has binding sites to three subunits: TRF1, TRF2, and TPP1. Here we identify a fourth partner, heterochromatin protein 1γ (HP1γ), that binds to a conserved canonical HP1-binding motif, PXVXL, in the C-terminal domain of TIN2. We show that HP1γ localizes to telomeres in S phase, where it is required to establish/maintain cohesion. We further demonstrate that the HP1-binding site in TIN2 is required for sister telomere cohesion and can impact telomere length maintenance by telomerase. Remarkably, the PTVML HP1-binding site is embedded in the recently identified cluster of mutations in TIN2 that gives rise to dyskeratosis congenita (DC), an inherited bone marrow failure syndrome caused by defects in telomere maintenance. We show that DC-associated mutations in TIN2 abrogate binding to HP1γ and that DC patient cells are defective in sister telomere cohesion. Our data indicate a novel requirement for HP1γ in the establishment/maintenance of cohesion at human telomeres and, furthermore, may provide insight into the mechanism of pathogenesis in TIN2-mediated DC.

Indexed as

Amino Acid SequenceCell LineChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneDyskeratosis CongenitaHeLa CellsHumansMaleMolecular Sequence DataMutationProtein BindingShelterin ComplexS PhaseTelomeraseTelomereTelomere-Binding ProteinsACD protein, humanChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneShelterin ComplexTelomeraseTelomere-Binding ProteinsTINF2 protein, human

Identifiers

PMID21865325
PMCPMC3175717
OpenAlexW2065529250

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.