Ubiquitylation of ε-COP by PIRH2 and regulation of the secretion of PSA

Satoru Maruyama, Naoto Miyajima, Miyuki Bohgaki, Tadasuke Tsukiyama, Masahiko Shigemura, Katsuya Nonomura, Shigetsugu Hatakeyama*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


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 languageEnglish (US)
Pages (from-to)73-82
Number of pages10
JournalMolecular and Cellular Biochemistry
Issue number1-2
StatePublished - Jan 2008


  • Androgen receptor
  • PIRH2
  • PSA
  • Ubiquitin
  • ε-COP

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology


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