Evidence map›Paper›PMID 25278026›Full record

ArticleThe Journal of biological chemistry2014

The 3'-5' DNA exonuclease TREX1 directly interacts with poly(ADP-ribose) polymerase-1 (PARP1) during the DNA damage response.

Takuya Miyazaki, Yong-Soo Kim, Jeongheon Yoon, Hongsheng Wang, Teruhiko Suzuki, Herbert C Morse

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

36 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  3. Autoinflammatory syndromes of STING and TREX1 dysfunction.The Journal of clinical investigation · 2026
    Review
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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.

Takuya MiyazakiFrom the Virology and Cellular Immunology Section, Laboratory of Immunogenetics, NIAID, National Institutes of Health, Rockville, Maryland 20852 and.
Yong-Soo KimFrom the Virology and Cellular Immunology Section, Laboratory of Immunogenetics, NIAID, National Institutes of Health, Rockville, Maryland 20852 and.
Jeongheon YoonFrom the Virology and Cellular Immunology Section, Laboratory of Immunogenetics, NIAID, National Institutes of Health, Rockville, Maryland 20852 and.
Hongsheng WangFrom the Virology and Cellular Immunology Section, Laboratory of Immunogenetics, NIAID, National Institutes of Health, Rockville, Maryland 20852 and.
Teruhiko SuzukiStem Cell Project Group, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506 Japan.
Herbert C MorseFrom the Virology and Cellular Immunology Section, Laboratory of Immunogenetics, NIAID, National Institutes of Health, Rockville, Maryland 20852 and hmorse@niaid.nih.gov.
Tokyo Metropolitan Institute of Medical Science · JP

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

The main function of the 3'-5' DNA exonuclease TREX1 is to digest cytosolic single-stranded DNA to prevent activation of cell-intrinsic responses to immunostimulatory DNA. TREX1 translocates to the nucleus following DNA damage with its nuclear activities being less well defined. Although mutations in human TREX1 have been linked to autoimmune/inflammatory diseases, the mechanisms contributing to the pathogenesis of these diseases remain incompletely understood. Here, using mass spectrometry and co-immunoprecipitation assays and in vivo overexpression models, we show that TREX1 interacts with poly(ADP-ribose) polymerase-1 (PARP1), a nuclear enzyme involved in the DNA damage response. Two zinc finger domains at the amino terminus of PARP1 were required for the interaction with TREX1 that occurs after nuclear translocation of TREX1 in response to DNA damage. Functional studies suggested that TREX1 may contribute to stabilization of PARP1 levels in the DNA damage response and its activity. These results provide new insights into the mechanisms of single-stranded DNA repair following DNA damage and alterations induced by gene mutations.

Indexed as

DNA DamageActive Transport, Cell NucleusBlotting, WesternCell NucleusDNA RepairDNA, Single-StrandedExodeoxyribonucleasesHEK293 CellsHeLa CellsHumansImmunoprecipitationK562 CellsMass SpectrometryMutationPhosphoproteinsPoly (ADP-Ribose) Polymerase-1DNA, Single-StrandedExodeoxyribonucleasesPARP1 protein, humanPhosphoproteinsPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerasesthree prime repair exonuclease 1Autoimmune DiseaseDNA Damage ResponseImmunologyInflammationPARP1Protein TranslocationTREX1

Identifiers

PMID25278026
PMCPMC4239609
OpenAlexW1983276280

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.