Evidence map›Paper›PMID 21437237›Full record

ArticlePloS one2011

Cooperative nuclear localization sequences lend a novel role to the N-terminal region of MSH6.

Natalie R Gassman, Jill E Clodfelter, Anita K McCauley, Keith Bonin, Freddie R Salsbury, Karin D Scarpinato

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Mismatch Repair Protein Msh6International journal of molecular sciences · 2023
    Article
  2. Article
  3. Review
  4. Article
  5. HDAC3 deacetylates the DNA mismatch repair factor MutSβ to stimulate triplet repeat expansions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Must Peutz-Jeghers syndrome patients have theWorld journal of clinical cases · 2018
    Article
  9. MutSFrontiers in physics · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
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.

Natalie R GassmanDepartment of Cancer Biology, Wake Forest University School of Medicine, Winston Salem, North Carolina, United States of America.
Jill E Clodfelter
Anita K McCauley
Keith Bonin
Freddie R Salsbury
Karin D Scarpinato
Wake Forest University · US

Funding

Tumor Tissue CoreP30CA012197 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Ruben A. Mesa · 1985 to 2026
$55.4M
Targeting the MSH2-dependent Apoptotic PathwayR01CA129373 · NCI · WAKE FOREST UNIVERSITY · PI SALSBURY, FREDDIE R. · 2009 to 2013
$1.6M
Repair Proteins: Interface between Cell Death &SurvivalR01CA101829 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI SCARPINATO, KARIN D. · 2005 to 2009
$1.2M
NCI NIH HHS 5R01CA12937NCI NIH HHS CA101829NCI NIH HHS P30 CA012197NCI NIH HHS R01 CA101829NCI NIH HHS R01 CA129373
6 · The paper itself

Abstract

Human mismatch repair proteins MSH2-MSH6 play an essential role in maintaining genetic stability and preventing disease. While protein functions have been extensively studied, the substantial amino-terminal region (NTR*) of MSH6 that is unique to eukaryotic proteins, has mostly evaded functional characterization. We demonstrate that a cluster of three nuclear localization signals (NLS) in the NTR direct nuclear import. Individual NLSs are capable of partially directing cytoplasmic protein into the nucleus; however only cooperative effects between all three NLSs efficiently transport MSH6 into the nucleus. In striking contrast to yeast and previous assumptions on required heterodimerization, human MSH6 does not determine localization of its heterodimeric partner, MSH2. A cancer-derived mutation localized between two of the three NLS significantly decreases nuclear localization of MSH6, suggesting altered protein localization can contribute to carcinogenesis. These results clarify the pending speculations on the functional role of the NTR in human MSH6 and identify a novel, cooperative nuclear localization signal.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceCell NucleusConserved SequenceDNA-Binding ProteinsGreen Fluorescent ProteinsHumansKineticsModels, BiologicalMolecular Sequence DataNeoplasmsNuclear Localization SignalsPoint MutationProtein MultimerizationRecombinant Fusion ProteinsReproducibility of ResultsDNA-Binding ProteinsGreen Fluorescent ProteinsG-T mismatch-binding proteinNuclear Localization SignalsRecombinant Fusion Proteins

Identifiers

PMID21437237
PMCPMC3060103
OpenAlexW2090301564

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.