Evidence map›Paper›PMID 17237827›Full record

ArticleOncogene2007

Energy-dependent nucleolar localization of p53 in vitro requires two discrete regions within the p53 carboxyl terminus.

O Karni-Schmidt, A Friedler, A Zupnick, K McKinney, M Mattia, R Beckerman, P Bouvet, M Sheetz, A Fersht, C Prives

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

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  11. DECOD: fast and accurate discriminative DNA motif finding.Bioinformatics (Oxford, England) · 2011
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 4 countries.

O Karni-SchmidtDepartment of Biological Sciences, Columbia University, New York, USA.
A Friedler
A Zupnick
K McKinney
M Mattia
R Beckerman
P Bouvet
M Sheetz
A Fersht
C Prives
Columbia University · USMedical Research Council · GBLaboratoire de Biologie et Modélisation de la Cellule · FR

Funding

Scientific ReagentsP01CA087497 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PRIVES, CAROL · 2000 to 2021
$35.4M
Regulation of the p53 tumor suppressor proteinR01CA058316 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PRIVES, CAROL · 1993 to 2017
$5.3M
REGULATION OF THE P53 TUMOR SUPPRESSOR PROTEINR37CA058316 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PRIVES, CAROL · 1998 to 2007
$3.8M
Medical Research Council MC_U105474168NCI NIH HHS CA58316NCI NIH HHS CA87497
6 · The paper itself

Abstract

The p53 tumor suppressor is a nucleocytoplasmic shuttling protein that is found predominantly in the nucleus of cells. In addition to mutation, abnormal p53 cellular localization is one of the mechanisms that inactivate p53 function. To further understand features of p53 that contribute to the regulation of its trafficking within the cell, we analysed the subnuclear localization of wild-type and mutant p53 in human cells that were either permeabilized with detergent or treated with the proteasome inhibitor MG132. We, here, show that either endogenously expressed or exogenously added p53 protein localizes to the nucleolus in detergent-permeabilized cells in a concentration- and ATP hydrolysis-dependent manner. Two discrete regions within the carboxyl terminus of p53 are essential for nucleolar localization in permeabilized cells. Similarly, localization of p53 to the nucleolus after proteasome inhibition in unpermeabilized cells requires sequences within the carboxyl terminus of p53. Interestingly, genotoxic stress markedly decreases the association of p53 with the nucleolus, and phosphorylation of p53 at S392, a site that is modified by such stress, partially impairs its nucleolar localization. The possible significance of these findings is discussed.

Indexed as

Adenosine TriphosphateBlotting, WesternCell NucleolusCells, CulturedCysteine Proteinase InhibitorsDetergentsDNA DamageFluorescent Antibody TechniqueHumansIn Vitro TechniquesLeupeptinsPermeabilityProteasome Endopeptidase ComplexProtein Structure, TertiaryProtein TransportTransfectionAdenosine Triphosphatebenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsDetergentsLeupeptinsProteasome Endopeptidase ComplexTumor Suppressor Protein p53

Identifiers

PMID17237827
OpenAlexW2040840144

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.