Evidence map›Paper›PMID 12697830›Full record

ArticleMolecular and cellular biology2003

Dimerization of MLH1 and PMS2 limits nuclear localization of MutLalpha.

Xiaosheng Wu, Jeffrey L Platt, Marilia Cascalho

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 74 citations in OpenAlex.

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  14. Analysis of clinically relevant somatic mutations in high-risk head and neck cutaneous squamous cell carcinoma.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2018
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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

3 authors at 1 institution in 1 country.

Xiaosheng WuTransplantation Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Jeffrey L Platt
Marilia Cascalho
Mayo Clinic · US

Funding

Xenogeneic Natural Antibody Targets-Structure/FunctionR37HL052297 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PLATT, JEFFREY L · 2001 to 2010
$3.9M
Elements of B Cell MemoryR01AI048602 · NIAID · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI CASCALHO, MARILIA ISABEL · 2001 to 2005
$1.5M
HEPARAN SULFATE IN CELLULAR IMMUNITY AND GRAFT REJECTIONR01HL046810 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI PLATT, JEFFREY L · 1991 to 2003
$1.4M
XENOGENEIC NATURAL ANTIBODY TARGETS--STRUCTURE/FUNCTIONR01HL052297 · NHLBI · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI PLATT, JEFFREY L · 1993 to 2000
$319k
NHLBI NIH HHS HL46810NHLBI NIH HHS HL52297NHLBI NIH HHS R01 HL046810NHLBI NIH HHS R01 HL052297NHLBI NIH HHS R37 HL052297NIAID NIH HHS AI48602NIAID NIH HHS R01 AI048602
6 · The paper itself

Abstract

DNA mismatch repair maintains genomic stability by detecting and correcting mispaired DNA sequences and by signaling cell death when DNA repair fails. The mechanism by which mismatch repair coordinates DNA damage and repair with cell survival or death is not understood, but it suggests the need for regulation. Since the functions of mismatch repair are initiated in the nucleus, we asked whether nuclear transport of MLH1 and PMS2 is limiting for the nuclear localization of MutLalpha (the MLH1-PMS2 dimer). We found that MLH1 and PMS2 have functional nuclear localization signals (NLS) and nuclear export sequences, yet nuclear import depended on their C-terminal dimerization to form MutLalpha. Our studies are consistent with the idea that dimerization of MLH1 and PMS2 regulates nuclear import by unmasking the NLS. Limited nuclear localization of MutLalpha may thus represent a novel mechanism by which cells fine-tune mismatch repair functions. This mechanism may have implications in the pathogenesis of hereditary non-polyposis colon cancer.

Indexed as

DNA Repair EnzymesActive Transport, Cell NucleusAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesAnimalsBase Pair MismatchBase SequenceCarrier ProteinsCell NucleusDimerizationDNA-Binding ProteinsDNA RepairEscherichia coli ProteinsHeLa CellsHumansMiceAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesCarrier ProteinsDNA-Binding ProteinsDNA Repair EnzymesEscherichia coli ProteinsMismatch Repair Endonuclease PMS2MLH1 protein, humanMlh1 protein, mouseMutL protein, E coliMutL Protein Homolog 1MutL ProteinsNeoplasm ProteinsNuclear Localization SignalsNuclear ProteinsPMS2 protein, humanPms2 protein, mouse

Identifiers

PMID12697830
PMCPMC153201
OpenAlexW2145285449

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.