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

@article{citeulike:2931242, 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 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.}, address = {Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, Japan.}, author = {Maruyama, S. and Miyajima, N. and Bohgaki, M. and Tsukiyama, T. and Shigemura, M. and Nonomura, K. and Hatakeyama, S.}, citeulike-article-id = {2931242}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s11010-007-9586-3}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17721809}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17721809}, doi = {10.1007/s11010-007-9586-3}, issn = {0300-8177}, journal = {Molecular and cellular biochemistry}, keywords = {cancer, coatomer, copi, in\_vivo, ubiquitination}, month = {January}, number = {1-2}, pages = {73--82}, posted-at = {2008-06-26 15:54:30}, priority = {2}, title = {Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA.}, url = {http://dx.doi.org/10.1007/s11010-007-9586-3}, volume = {307}, year = {2008} }

TY - JOUR ID - citeulike:2931242 L3 - citeulike-article-id:2931242 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 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. IS - 1-2 JF - Molecular and cellular biochemistry SN - 0300-8177 AD - Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido, Japan. EP - 82 TI - Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. VL - 307 SP - 73 KW - cancer KW - coatomer KW - copi KW - in_vivo KW - ubiquitination AU - Maruyama, S AU - Miyajima, N AU - Bohgaki, M AU - Tsukiyama, T AU - Shigemura, M AU - Nonomura, K AU - Hatakeyama, S PY - 2008/01// UR - http://dx.doi.org/10.1007/s11010-007-9586-3 ER -