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Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA
Title: | Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA |
Authors: | Maruyama, Satoru Browse this author | Miyajima, Naoto Browse this author | Bohgaki, Miyuki Browse this author | Tsukiyama, Tadasuke Browse this author | Shigemura, Masahiko Browse this author | Nonomura, Katsuya Browse this author | Hatakeyama, Shigetsugu Browse this author →KAKEN DB |
Keywords: | PIRH2 | ε-COP | ubiquitin | androgen receptor | PSA |
Issue Date: | Jan-2008 |
Publisher: | Springer |
Journal Title: | Molecular and Cellular Biochemistry |
Volume: | 307 |
Issue: | 1-2 |
Start Page: | 73 |
End Page: | 82 |
Publisher DOI: | 10.1007/s11010-007-9586-3 |
PMID: | 17721809 |
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. |
Rights: | The original publication is available at www.springerlink.com |
Relation: | http://www.springerlink.com |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/32324 |
Appears in Collections: | 医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 畠山 鎮次
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