Evidence map›Paper›PMID 19282665›Full record

ArticleCell cycle (Georgetown, Tex.)2009

Homeodomain protein Dlx3 induces phosphorylation-dependent p63 degradation.

Antonella Di Costanzo, Luisa Festa, Olivier Duverger, Maria Vivo, Luisa Guerrini, Girolama La Mantia, Maria I Morasso, Viola Calabrò

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. The dual role of p63 in cancer.Frontiers in oncology · 2023
    Review
  2. Review
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  7. The Regulation of Tumor Suppressor p63 by the Ubiquitin-Proteasome System.International journal of molecular sciences · 2016
    Review
  8. Article
  9. Article
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  12. Modeling AEC-New approaches to study rare genetic disorders.American journal of medical genetics. Part A · 2014
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Antonella Di CostanzoDepartment of Structural and Molecular Biology, University of Naples, Naples, Italy.
Luisa Festa
Olivier Duverger
Maria Vivo
Luisa Guerrini
Girolama La Mantia
Maria I Morasso
Viola Calabrò
Universidad Nacional De Caaguazú · PYUniversity of Naples Federico II · IT

Funding

Ectodermal Dysplasias and Regulation of Ectodermal Appendage DevelopmentZIAAR041171 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI MORASSO, MARIA · 2009 to 2024
$10.8M
Intramural NIH HHS ZIA AR041171Telethon GGP030326Telethon GGP05056
6 · The paper itself

Abstract

The epidermis is a stratified epithelium which develops depending on the transcription factor p63, a member of the p53 family of transcription factors. p63 is strongly expressed in the innermost basal layer where highly proliferative epithelial cells reside. p63 functions as a molecular switch that initiates epithelial stratification or cell fate determination while regulating proliferation and differentiation of developmentally mature keratinocytes. p63 acts upstream of Dlx3 homeobox gene in a transcriptional regulatory pathway relevant to ectodermal dysplasia. Here we show that Dlx3 triggers p63 protein degradation by a proteasome-dependent pathway. Mutant DeltaNp63alpha in which Threonine397 and Serine383 were replaced with Alanine as well as C-terminal truncated versions of DeltaNp63alpha are resistant to Dlx3-mediated degradation. Transient expression of Dlx3 is associated with Raf1 phosphorylation. Dlx3 is unable to promote p63 degradation in Raf1 depleted MEF cells or upon pharmacological knockdown of Raf1. Our data support a previously unrecognized role for Dlx3 in posttranslational regulation of DeltaNp63alpha protein level, a mechanism that may contribute to reduce the abundance of DeltaNp63alpha during differentiation of stratified epithelia.

Indexed as

Protein Processing, Post-TranslationalAmino AcidsAmino Acid SequenceAnimalsCell LineDown-RegulationHalf-LifeHomeodomain ProteinsHumansKeratinocytesMiceMolecular Sequence DataPhosphorylationProteasome Endopeptidase ComplexProtein Bindingraf KinasesAmino AcidsDistal-less homeobox proteinsHomeodomain ProteinsProteasome Endopeptidase Complexraf KinasesTP63 protein, humanTrans-ActivatorsTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID19282665
PMCPMC2803028
OpenAlexW1965849475

What OpenQuestion holds

Textmetadata
LicenceTDM
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.