Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA.

Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Research Abstract Details 

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Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Abstract Text:

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

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.

Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Publishing Authors By Initials

S Maruyama,N Miyajima,M Bohgaki,T Tsukiyama,M Shigemura,K Nonomura,S Hatakeyama,S Maruyama,N Miyajima,M Bohgaki,T Tsukiyama,M Shigemura,K Nonomura,S Hatakeyama,

For similar biochemical phenomena, metabolism, and nutrition: metabolism: ubiquitination research abstracts see: biochemical phenomena, metabolism, and nutrition: metabolism: ubiquitination research

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Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular and cellular biochemistry

VOLUME: 307

Page Numbers: 73-82

Journal Abbreviation: Mol. Cell. Biochem.

ISSN: 0300-8177

DAY: 25

MONTH: 08

YEAR: 2007

Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Information

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LANGUAGE: eng

NlmUniqueID: 364456

Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Keywords Mesh Terms:

KEYWORDS: Ubiquitination

MESH TERMS: metabolism

Chemical & Substance for Abstract: Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Information

Substance Name: Ubiquitin-Protein Ligases

Registry Number: EC 6.3.2.19

Grant and Affiliation Information for Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA.

AFFILIATION: Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, Japan.

Country: Netherlands

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MEDLINETA: Mol Cell Biochem

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