ArticlePloS one2013
The homeodomain transcription factor Hoxa2 interacts with and promotes the proteasomal degradation of the E3 ubiquitin protein ligase RCHY1.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Antioxidant and Photoprotective Activities of 3,4-Dihydroxybenzoic Acid and (+)-Catechin, Identified fromAntioxidants (Basel, Switzerland) · 2025Article
- Homeodomain Involvement in Nuclear HOX Protein Homo- and Heterodimerization.International journal of molecular sciences · 2025Article
- Deciphering the emerging landscape of HOX genes in cardiovascular biology, atherosclerosis and beyond (Review).International journal of molecular medicine · 2024Article
- The Role of E3 Ligase Pirh2 in Disease.Cells · 2022Review
- HOX Protein Activity Regulation by Cellular Localization.Journal of developmental biology · 2021Review
- HOXA1 Is an Antagonist of ERα in Breast Cancer.Frontiers in oncology · 2021Article
- HOX paralogs selectively convert binding of ubiquitous transcription factors into tissue-specific patterns of enhancer activation.PLoS genetics · 2020Article
- HOXA1 binds RBCK1/HOIL-1 and TRAF2 and modulates the TNF/NF-κB pathway in a transcription-independent manner.Nucleic acids research · 2016Article
- Review
- Article
- Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation.Biomolecules · 2014Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hox proteins are conserved homeodomain transcription factors known to be crucial regulators of animal development. As transcription factors, the functions and modes of action (co-factors, target genes) of Hox proteins have been very well studied in a multitude of animal models. However, a handful of reports established that Hox proteins may display molecular activities distinct from gene transcription regulation. Here, we reveal that Hoxa2 interacts with 20S proteasome subunits and RCHY1 (also known as PIRH2), an E3 ubiquitin ligase that targets p53 for degradation. We further show that Hoxa2 promotes proteasome-dependent degradation of RCHY1 in an ubiquitin-independent manner. Correlatively, Hoxa2 alters the RCHY1-mediated ubiquitination of p53 and promotes p53 stabilization. Together, our data establish that Hoxa2 can regulate the proteasomal degradation of RCHY1 and stabilization of p53.
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Registered trials
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.