Identification of a novel post-translational modification of epidermal growth factor domains and mechanistic analysis of the modification
| Project/Area Number |
21790270
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
General medical chemistry
|
|---|
| Research Institution | Nagoya University |
|---|
Principal Investigator |
OKAJIMA Tetsuya Nagoya University, 医学系研究科, 准教授 (20420383)
|
|---|
| Project Period (FY) |
2009 – 2010
|
| Project Status |
Completed (Fiscal Year 2010)
|
| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2009: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
|
|---|
| Keywords | Notch受容体 / 糖鎖修飾 / O-結合型糖鎖 / O-GlcNAc / Notch / 糖転移酵素 |
|---|
| Research Abstract |
Epidermal growth factor (EGF) domains are posttranslationally modified with unique O-linked glycans. The classical types of O-glycans on EGF domains are O-fucose and O-glucose glycans, found on many plasma glycoproteins and signaling molecules, whose biological functions have been demonstrated especially in the context of the Notch signaling pathway. In this study, we have discovered O-GlcNAc modification as a new modification of the EGF domain that occurs on the conserved Ser/Thr residue located between the fifth and sixth cysteine residues within the EGF domains of Notch receptors in Drosophila. Moreover, we have succeeded in the isolation of a new gene, Eogt, responsible for the extracellular O-GlcNAcylation. Characterization of physiological function of Eogt will reveal the new biological roles for O-GlcNAcylation in the extracellular environment.
|
Report
(3 results)
Research Products
(17 results)
