ArticleMolecular and cellular biochemistry2008
Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA.
Article in Molecular and cellular biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed, 14 citations in OpenAlex.
- Post-Translational Modifications That Drive Prostate Cancer Progression.Biomolecules · 2021Review
- Directing Traffic: Regulation of COPI Transport by Post-translational Modifications.Frontiers in cell and developmental biology · 2019Review
- The E3 ligase PIRH2 polyubiquitylates CHK2 and regulates its turnover.Cell death and differentiation · 2013Article
- Pirh2 RING-finger E3 ubiquitin ligase: its role in tumorigenesis and cancer therapy.FEBS letters · 2012Review
- The p73 tumor suppressor is targeted by Pirh2 RING finger E3 ubiquitin ligase for the proteasome-dependent degradation.The Journal of biological chemistry · 2011Article
- A novel oncoprotein Pirh2: rising from the shadow of MDM2.Cancer science · 2011Review
- High expression of Pirh2, an E3 ligase for p27, is associated with low expression of p27 and poor prognosis in head and neck cancers.Cancer science · 2009Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitylation appears to be involved in the membrane trafficking system including endocytosis, exocytosis, and ER-to-Golgi transport. We found that PIRH2, which was identified as an interacting protein for androgen receptor or p53, interacts with and ubiquitylates the epsilon-subunit of coatmer complex, epsilon-COP. PIRH2 promotes the ubiquitylation of epsilon-COP in vitro and in vivo and consequently promotes the degradation of epsilon-COP. The interaction between PIRH2 and epsilon-COP is affected by the presence of androgen, and PIRH2 in the presence of androgen promotes ubiquitylation of epsilon-COP in vivo. Furthermore, overexpression of the wild type of PIRH2 in prostate cancer cells causes downregulation of the secretion of prostate-specific antigen (PSA), a secretory protein in prostate epithelial cells and one of diagnostic markers for prostate cancer. Our results indicate that PIRH2 functions as a regulator for COP I complex.
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Registered trials
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