Evidence map›Paper›PMID 23382381›Full record

ArticleThe Journal of biological chemistry2013

Supervillin-mediated suppression of p53 protein enhances cell survival.

Zhiyou Fang, Elizabeth J Luna

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Zhiyou FangDepartment of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605. Electronic address: zhiyou.fang@umassmed.edu.
Elizabeth J LunaDepartment of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605. Electronic address: elizabeth.luna@umassmed.edu.
University of Massachusetts Chan Medical School · US

Funding

CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
NIGMS NIH HHS GM033048-26S1NIGMS NIH HHS R01 GM033048
6 · The paper itself

Abstract

Integrin-based adhesions promote cell survival as well as cell motility and invasion. We show here that the adhesion regulatory protein supervillin increases cell survival by decreasing levels of the tumor suppressor protein p53 and downstream target genes. RNAi-mediated knockdown of a new splice form of supervillin (isoform 4) or both isoforms 1 and 4 increases the amount of p53 and cell death, whereas p53 levels decrease after overexpression of either supervillin isoform. Cellular responses to DNA damage induced by etoposide or doxorubicin include down-regulation of endogenous supervillin coincident with increases in p53. In DNA-damaged supervillin knockdown cells, p53 knockdown or inhibition partially rescues the loss of cell metabolic activity, a measure of cell proliferation. Knockdown of the p53 deubiquitinating enzyme USP7/HAUSP also reverses the supervillin phenotype, blocking the increase in p53 levels seen after supervillin knockdown and accentuating the decrease in p53 levels triggered by supervillin overexpression. Conversely, supervillin overexpression decreases the association of USP7 and p53 and attenuates USP7-mediated p53 deubiquitination. USP7 binds directly to the supervillin N terminus and can deubiquitinate and stabilize supervillin. Supervillin also is stabilized by derivatization with the ubiquitin-like protein SUMO1. These results show that supervillin regulates cell survival through control of p53 levels and suggest that supervillin and its interaction partners at sites of cell-substrate adhesion constitute a locus for cross-talk between survival signaling and cell motility pathways.

Indexed as

Cell AdhesionCell Line, TumorCell ProliferationCell SurvivalCloning, MolecularCytoskeletonDNA DamageFocal Adhesion Protein-Tyrosine KinasesGenetic VectorsHEK293 CellsHeLa CellsHumansMembrane ProteinsMicrofilament ProteinsMicroscopy, FluorescenceModels, BiologicalFocal Adhesion Protein-Tyrosine KinasesMembrane ProteinsMicrofilament ProteinsProtein IsoformsSVIL protein, humanTP53 protein, humanTumor Suppressor Protein p53UbiquitinUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, human

Identifiers

PMID23382381
PMCPMC3597829
OpenAlexW2026437259

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.