Evidence map›Paper›PMID 19282251›Full record

ArticleDNA repair2009

Reciprocal regulation of nuclear import of the yeast MutSalpha DNA mismatch repair proteins Msh2 and Msh6.

Alicia P Hayes, Leah A Sevi, Megan C Feldt, Mark D Rose, Alison E Gammie

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2009. 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
1.6field-weighted citation impact, top 18% 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, 19 citations in OpenAlex.

  1. Review
  2. Mismatch Repair Protein Msh6International journal of molecular sciences · 2023
    Article
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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

5 authors at 1 institution in 1 country.

Alicia P HayesDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, United States.
Leah A Sevi
Megan C Feldt
Mark D Rose
Alison E Gammie
Princeton University · US

Funding

Mechanisms of Nuclear and Cell Fusion in YeastR01GM037739 · NIGMS · PRINCETON UNIVERSITY · PI ROSE, MARK DAVID · 1987 to 2016
$7.4M
NIGMS NIH HHS GM037739NIGMS NIH HHS R01 GM037739
6 · The paper itself

Abstract

DNA mismatch recognition is performed in eukaryotes by two heterodimers known as MutSalpha (Msh2/Msh6) and MutSbeta (Msh2/Msh3) that must reside in the nucleus to function. Two putative Msh2 nuclear localization sequences (NLS) were characterized by fusion to green fluorescent protein (GFP) and site-directed mutagenesis in the context of Msh2. One NLS functioned in GFP targeting assays and both acted redundantly within Msh2. We examined nuclear localization of each of the MutS monomers in the presence and absence of their partners. Msh2 translocated to the nucleus in cells lacking Msh3 and Msh6; however, cells lacking Msh6 showed significantly decreased levels of nuclear Msh2. Furthermore, the overall protein levels of Msh2 were significantly diminished in the absence of Msh6, particularly if Msh2 lacked a functional NLS. Msh3 localized in the absence of Msh2, but Msh6 localization depended on Msh2 expressing functional NLSs. Overall, the nuclear levels of Msh2 and Msh6 decline when the other partner is absent. The data suggest a stabilization mechanism to prevent free monomer accumulation in the cytoplasm.

Indexed as

Active Transport, Cell NucleusCell NucleusCytoplasmDNA-Binding ProteinsDNA RepairFluorescent Antibody Technique, IndirectGreen Fluorescent ProteinsImmunoblottingMutagenesis, Site-DirectedMutS Homolog 2 ProteinProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesDNA-Binding ProteinsGreen Fluorescent ProteinsMSH2 protein, S cerevisiaeMSH6 protein, S cerevisiaeMutS Homolog 2 ProteinSaccharomyces cerevisiae Proteins

Identifiers

PMID19282251
PMCPMC2728017
OpenAlexW2065627776

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.