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

doi:10.1007/s11010-007-9586-3

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

Medicine, Pulmonary Division

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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)
Pages (from-to)	73-82
Number of pages	10
Journal	Molecular and Cellular Biochemistry
Volume	307
Issue number	1-2
DOIs	https://doi.org/10.1007/s11010-007-9586-3
State	Published - Jan 2008

Keywords

Androgen receptor
PIRH2
PSA
Ubiquitin
ε-COP

ASJC Scopus subject areas

Molecular Biology
Clinical Biochemistry
Cell Biology

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title = "Ubiquitylation of ε-COP by PIRH2 and regulation of the secretion of PSA",

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.",

keywords = "Androgen receptor, PIRH2, PSA, Ubiquitin, ε-COP",

author = "Satoru Maruyama and Naoto Miyajima and Miyuki Bohgaki and Tadasuke Tsukiyama and Masahiko Shigemura and Katsuya Nonomura and Shigetsugu Hatakeyama",

note = "Funding Information: Acknowledgments We thank G. Sobue and T. Kitamura for the plasmids and cell lines and Y. Soida for helping with the preparation of the manuscript. The work was supported in part by a research grant from Grant-in-Aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology (18013001), the Osaka Cancer Research Foundation and the Akiyama Foundation.",

year = "2008",

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doi = "10.1007/s11010-007-9586-3",

language = "English (US)",

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AU - Maruyama, Satoru

AU - Miyajima, Naoto

AU - Bohgaki, Miyuki

AU - Tsukiyama, Tadasuke

AU - Shigemura, Masahiko

AU - Nonomura, Katsuya

AU - Hatakeyama, Shigetsugu

N1 - Funding Information: Acknowledgments We thank G. Sobue and T. Kitamura for the plasmids and cell lines and Y. Soida for helping with the preparation of the manuscript. The work was supported in part by a research grant from Grant-in-Aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology (18013001), the Osaka Cancer Research Foundation and the Akiyama Foundation.

PY - 2008/1

Y1 - 2008/1

N2 - 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.

AB - 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.

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

Abstract

Keywords

ASJC Scopus subject areas

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