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 ε-subunit of coatmer complex, ε-COP. PIRH2 promotes the ubiquitylation of ε-COP in vitro and in vivo and consequently promotes the degradation of ε-COP. The interaction between PIRH2 and ε-COP is affected by the presence of androgen, and PIRH2 in the presence of androgen promotes ubiquitylation of ε-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.
Original language | English (US) |
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Pages (from-to) | 73-82 |
Number of pages | 10 |
Journal | Molecular and Cellular Biochemistry |
Volume | 307 |
Issue number | 1-2 |
DOIs | |
State | Published - Jan 2008 |
Keywords
- Androgen receptor
- PIRH2
- PSA
- Ubiquitin
- ε-COP
ASJC Scopus subject areas
- Molecular Biology
- Clinical Biochemistry
- Cell Biology