2011 Fiscal Year Final Research Report
Cellular role and regulatory mechanism for a novel deubiquitinating enzyme in the endoplasmic reticulum
Project/Area Number |
22770123
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Single-year Grants |
Research Field |
Functional biochemistry
|
Research Institution | Tokyo Institute of Technology |
Principal Investigator |
NAKAMURA Nobuhiro 東京工業大学, 大学院・生命理工学研究科, 准教授 (80361765)
|
Project Period (FY) |
2010 – 2011
|
Keywords | 小胞体 / 脱ユビキチン化 / プロテアソーム分解 |
Research Abstract |
This study has demonstrated that 1) USP19, a transmembrane deubiquitinating enzyme in the endoplasmic reticulum(ER), deubiquitinates not only typical substrates of ER-associated degradation(ERAD), but also ERAD ubiquitinating enzymes, and 2) the enzymatic activity of USP19 is dependent on the domain structures and processing of USP19. These results provide better understand of the molecular mechanism for the regulation of the ERAD pathway as well as the USP19 activity.
|
Research Products
(7 results)
-
[Journal Article] Identification of SAMT family proteins as substrates of MARCH11 in mouse spermatids2012
Author(s)
Yogo, K., Tojima, H., Ohno, J. Y., Ogawa, T., Nakamura, N., Hirose, S., Takeya, T., & Kohsaka, T.
-
Journal Title
Histochem. Cell Biol
Volume: 137
Pages: 53-65
Peer Reviewed
-
-
-
[Journal Article] Identification of zebrafish FXYD11a protein that is highly expressed in ion-transporting epithelium of the gill and skin and its possible role in ion homeostasis2010
Author(s)
Saito, K., Nakamura, N., Ito, Y., Hoshijima, K., Esaki, M. Zhao, B., & Hirose, S.
-
Journal Title
Front. Physio
Volume: 1
Pages: 129
Peer Reviewed
-
-
-