Evidence map›Paper›PMID 24984242›Full record

ArticleDNA repair2014

DNA Ligase IV regulates XRCC4 nuclear localization.

Dailia B Francis, Mikhail Kozlov, Jose Chavez, Jennifer Chu, Shruti Malu, Mary Hanna, Patricia Cortes

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Phosphorylation and DNA damage resolution coordinate SOX2-mediated reprogramming in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

7 authors at 1 institution in 1 country.

Dailia B FrancisImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Graduate School of Biological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States.
Mikhail KozlovImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States.
Jose ChavezImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States.
Jennifer ChuImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States.
Shruti MaluImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States.
Mary HannaImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States.
Patricia CortesImmunology Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Graduate School of Biological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States. Electronic address: Patricia.Cortes@mssm.edu.
Icahn School of Medicine at Mount Sinai · US

Funding

Regulation of V(D)J recombination by Rag2 C terminusR01AI070880 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI CORTES, PATRICIA · 2010 to 2014
$1.6M
Mechanism and regulation of V(D)J repairR01AI080755 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI CORTES, PATRICIA · 2009 to 2013
$1.6M
NIAID NIH HHS R01 AI070880NIAID NIH HHS R01 AI080755PHS HHS 5T32A1007605-10PHS HHS T32-A1007605-09
6 · The paper itself

Abstract

DNA Ligase IV, along with its interacting partner XRCC4, are essential for repairing DNA double strand breaks by non-homologous end joining (NHEJ). Together, they complete the final ligation step resolving the DNA break. Ligase IV is regulated by XRCC4 and XLF. However, the mechanism(s) by which Ligase IV control the NHEJ reaction and other NHEJ factor(s) remains poorly characterized. Here, we show that a C-terminal region of Ligase IV (aa 620-800), which encompasses a NLS, the BRCT I, and the XRCC4 interacting region (XIR), is essential for nuclear localization of its co-factor XRCC4. In Ligase IV deficient cells, XRCC4 showed deregulated localization remaining in the cytosol even after induction of DNA double strand breaks. DNA Ligase IV was also required for efficient localization of XLF into the nucleus. Additionally, human fibroblasts that harbor hypomorphic mutations within the Ligase IV gene displayed decreased levels of XRCC4 protein, implicating that DNA Ligase IV is also regulating XRCC4 stability. Our results provide evidence for a role of DNA Ligase IV in controlling the cellular localization and protein levels of XRCC4.

Indexed as

Active Transport, Cell NucleusBinding SitesCell LineCell NucleusDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA Ligase ATPDNA LigasesDNA Repair EnzymesFibroblastsHumansLymphocytesNuclear Localization SignalsDNA-Binding ProteinsDNA Ligase ATPDNA LigasesDNA Repair EnzymesLIG4 protein, humanNHEJ1 protein, humanNuclear Localization SignalsXRCC4 protein, humanDNA Ligase IVDNA repairNHEJV(D)J recombinationXRCC4

Identifiers

PMID24984242
PMCPMC4151352
OpenAlexW1972354683

What OpenQuestion holds

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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.