Generation mechanism of free oligosaccharides in the lumen of the endoplasmic reticulum
| Project/Area Number |
24770134
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Functional biochemistry
|
|---|
| Research Institution | Institute of Physical and Chemical Research |
|---|
Principal Investigator |
HARADA Yoichiro 独立行政法人理化学研究所, 糖鎖代謝学研究チーム, 特別研究員 (80464147)
|
|---|
| Project Period (FY) |
2012-04-01 – 2014-03-31
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
|---|
| Keywords | 糖鎖代謝 / オリゴ糖転移酵素 / ドリコール結合型糖鎖 / 糖鎖生物学 / 遊離糖鎖 |
|---|
| Research Abstract |
In this study, I identified an enzyme involved in the metabolism of glycans in the lumen of the endoplasmic reticulum. Asparagine (N)-linked glycosylation is one of the posttranslational modifications, which modulates protein folding and degradation. The enzyme that mediates N-glycosylation is called oligosaccharyltransferase (OST). This enzyme transfers dolichol-linked oligosaccharides (DLOs) onto the specific asparagine residue of proteins. This study uncovered that OST also mediates a hydrolysis of DLOs in budding yeast and mammalian cells.This enzymatic activity has been known for over 30 years, but the responsible enzyme and its biological function were unknown. This study established the molecular basis of the DLO degradation, and opens an new avenue for understanding the biological functions of this novel glycan metabolic pathway.
|
Report
(3 results)
Research Products
(14 results)
-
-
-
-
-
-
-
-
-
-
-
-
-
-
[Book] Handbook of Glycosyltransferases and Related Genes2014
Author(s)
Taniguchi, N., Honke, K., Fukuda, M., Narimatsu, H., Yamaguchi, Y., Angata, T. (Eds.)
Total Pages
670
Publisher
Springer
Related Report
