Evidence map›Paper›PMID 24196442›Full record

ArticleCell cycle (Georgetown, Tex.)2014

CGGBP1 phosphorylation constitutes a telomere-protection signal.

Umashankar Singh, Varun Maturi, Rhiannon E Jones, Ylva Paulsson, Duncan M Baird, Bengt Westermark

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. CGGBP1 regulates CTCF occupancy at repeats.Epigenetics & chromatin · 2019
    Article
  8. Article
  9. Defining the role of the CGGBP1 protein in FMR1 gene expression.European journal of human genetics : EJHG · 2016
    Article
  10. Article
  11. Article
  12. Review
  13. Article
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 4 institutions in 3 countries.

Umashankar SinghDepartment of Immunology, Genetics, and Pathology; Uppsala University; Tumor Biology; Rudbeck Laboratory; Uppsala, Sweden.
Varun MaturiDepartment of Immunology, Genetics, and Pathology; Uppsala University; Tumor Biology; Rudbeck Laboratory; Uppsala, Sweden; Ludwig Institute for Cancer Research; Science for Life Laboratory; Uppsala University; Biomedical Center; Uppsala, Sweden.
Rhiannon E JonesDepartment of Pathology; School of Medicine; Cardiff University; Cardiff, UK.
Ylva PaulssonDepartment of Immunology, Genetics, and Pathology; Uppsala University; Tumor Biology; Rudbeck Laboratory; Uppsala, Sweden.
Duncan M BairdDepartment of Pathology; School of Medicine; Cardiff University; Cardiff, UK.
Bengt WestermarkDepartment of Immunology, Genetics, and Pathology; Uppsala University; Tumor Biology; Rudbeck Laboratory; Uppsala, Sweden.
Uppsala University · SECardiff University · GBIndiana University School of MedicinePediatrics and Genetics · US

Funding

Cancer Research UK C17199/A13490
6 · The paper itself

Abstract

The shelterin proteins are required for telomere integrity. Shelterin dysfunction can lead to initiation of unwarranted DNA damage and repair pathways at chromosomal termini. Interestingly, many shelterin accessory proteins are involved in DNA damage signaling and repair. We demonstrate here that in normal human fibroblasts, telomeric ends are protected by phosphorylation of CGG triplet repeat-binding protein 1 (CGGBP1) at serine 164 (S164). We show that serine 164 is a major phosphorylation site on CGGBP1 with important functions. We provide evidence that one of the kinases that can phosphorylate S164 CGGBP1 is ATR. Overexpression of S164A phospho-deficient CGGBP1 exerted a dominant-negative effect, causing telomeric dysfunction, accelerated telomere shortening, enhanced fusion of telomeres, and crisis. However, overexpression of wild-type or phospho-mimicking S164E CGGBP1 did not cause these effects. This telomere damage was associated with reduced binding of the shelterin protein POT1 to telomeric DNA. Our results suggest that CGGBP1 phosphorylation at S164 is a novel telomere protection signal, which can affect telomere-protective function of the shelterin complex.

Indexed as

Cell Cycle ProteinsDNA-Binding ProteinsDNA DamageGene Expression RegulationHumansPhosphorylationSerineShelterin ComplexSignal TransductionTelomereTelomere-Binding ProteinsCell Cycle ProteinsCGGBP1 protein, humanDNA-Binding ProteinsSerineShelterin ComplexTelomere-Binding ProteinsCGGBP1DNA damagePOT1telomere fusionsTelomeres

Identifiers

PMID24196442
PMCPMC3925742
OpenAlexW2079957285

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.