Evidence map›Paper›PMID 31182712›Full record

ArticleNature communications2019

Rif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane.

Gabriele A Fontana, Daniel Hess, Julia K Reinert, Stefano Mattarocci, Benoît Falquet, Dominique Klein, David Shore, Nicolas H Thomä, Ulrich Rass

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

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  19. The Many Faces of Lipids in Genome Stability (and How to Unmask Them).International journal of molecular sciences · 2021
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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

9 authors at 5 institutions in 3 countries.

Gabriele A FontanaFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0001-7697-6833
Daniel HessFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-1642-5404
Julia K ReinertFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0001-5932-4825
Stefano MattarocciDepartment of Molecular Biology and Institute of Genetics and Genomics in Geneva (iGE3), University of Geneva, 30 Quai Ernest-Ansermet, CH-1211, Geneva, Switzerland.
Benoît FalquetFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-4434-3799
Dominique KleinFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.
David ShoreDepartment of Molecular Biology and Institute of Genetics and Genomics in Geneva (iGE3), University of Geneva, 30 Quai Ernest-Ansermet, CH-1211, Geneva, Switzerland.ORCID http://orcid.org/0000-0002-9859-143X
Nicolas H ThomäFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.ORCID http://orcid.org/0000-0003-2685-906X
Ulrich RassFriedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland. U.W.Rass@sussex.ac.uk.ORCID http://orcid.org/0000-0001-9275-9062
Friedrich Miescher Institute · CHUniversity of Basel · CHUniversity of Geneva · CHBoard of the Swiss Federal Institutes of Technology · CHUniversity of Sussex · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rif1 is involved in telomere homeostasis, DNA replication timing, and DNA double-strand break (DSB) repair pathway choice from yeast to human. The molecular mechanisms that enable Rif1 to fulfill its diverse roles remain to be determined. Here, we demonstrate that Rif1 is S-acylated within its conserved N-terminal domain at cysteine residues C466 and C473 by the DHHC family palmitoyl acyltransferase Pfa4. Rif1 S-acylation facilitates the accumulation of Rif1 at DSBs, the attenuation of DNA end-resection, and DSB repair by non-homologous end-joining (NHEJ). These findings identify S-acylation as a posttranslational modification regulating DNA repair. S-acylated Rif1 mounts a localized DNA-damage response proximal to the inner nuclear membrane, revealing a mechanism of compartmentalized DSB repair pathway choice by sequestration of a fatty acylated repair factor at the inner nuclear membrane.

Indexed as

DNA Breaks, Double-StrandedDNA End-Joining RepairAcylationDNA RepairNuclear EnvelopeRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomere-Binding ProteinsRepressor ProteinsRIF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTelomere-Binding Proteins

Identifiers

PMID31182712
PMCPMC6557901
OpenAlexW2948672241

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.