Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA.
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.
Mesh Terms:
Androgens, Cells, Cultured, Coat Protein Complex I, Coatomer Protein, Dihydrotestosterone, Hela Cells, Humans, Male, Models, Biological, Prostate-Specific Antigen, Prostatic Neoplasms, Protein Binding, Protein Processing, Post-Translational, Protein Transport, Tissue Distribution, Ubiquitin-Protein Ligases, Ubiquitination
Androgens, Cells, Cultured, Coat Protein Complex I, Coatomer Protein, Dihydrotestosterone, Hela Cells, Humans, Male, Models, Biological, Prostate-Specific Antigen, Prostatic Neoplasms, Protein Binding, Protein Processing, Post-Translational, Protein Transport, Tissue Distribution, Ubiquitin-Protein Ligases, Ubiquitination
Mol. Cell. Biochem.
Date: Jan. 01, 2008
PubMed ID: 17721809
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