| Item type |
デフォルトアイテムタイプ_（フル）(1) |
| 公開日 |
2023-03-18 |
| タイトル |
|
|
タイトル |
Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan |
|
言語 |
en |
| 作成者 |
Nakano, Miyako
Mishra, Sushil K.
Tokoro, Yuko
Sato, Keiko
Nakajima, Kazuki
Yamaguchi, Yoshiki
Taniguchi, Naoyuki
Kizuka, Yasuhiko
|
| アクセス権 |
|
|
アクセス権 |
open access |
|
アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利情報 |
|
|
権利情報 |
This research was originally published in Molecular & Cellular Proteomics. Miyako Nakano, Sushil K. Mishra, Yuko Tokoro, Keiko Sato, Kazuki Nakajima, Yoshiki Yamaguchi, Naoyuki Taniguchi, Yasuhiko Kizuka. Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan. Mol Cell Proteomics. 2019; Vol 18: pp2044-pp2057. © the American Society for Biochemistry and Molecular Biology |
| 権利情報 |
|
|
権利情報 |
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認、ご利用ください。 |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Glycomics |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
glycoprotein pathways |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
glycosylation |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
glycoproteins |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
glycoprotein structure |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
glycoproteomics |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
bisecting GlcNAc |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
fucosylation |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
GnT-III |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
HNK-1 |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
sialylation |
| 内容記述 |
|
|
内容記述 |
Glycoproteins are decorated with complex glycans for protein functions. However, regulation mechanisms of complex glycan biosynthesis are largely unclear. Here we found that bisecting GlcNAc, a branching sugar residue in N-glycan, suppresses the biosynthesis of various types of terminal epitopes in N-glycans, including fucose, sialic acid and human natural killer-1. Expression of these epitopes in N-glycan was elevated in mice lacking the biosynthetic enzyme of bisecting GlcNAc, GnT-III, and was conversely suppressed by GnT-III overexpression in cells. Many glycosyltransferases for N-glycan terminals were revealed to prefer a nonbisected N-glycan as a substrate to its bisected counterpart, whereas no up-regulation of their mRNAs was found. This indicates that the elevated expression of the terminal N-glycan epitopes in GnT-III-deficient mice is attributed to the substrate specificity of the biosynthetic enzymes. Molecular dynamics simulations further confirmed that nonbisected glycans were preferentially accepted by those glycosyltransferases. These findings unveil a new regulation mechanism of protein N-glycosylation. |
|
言語 |
en |
| 内容記述 |
|
|
内容記述タイプ |
Other |
|
内容記述 |
This work was supported by Grant-in-Aid for Scientific Research (C) to Y.K. [17K07356], Leading Initiative for Excellent Young Researchers (LEADER) project to Y.K. from the Japan Society for the Promotion of Science (JSPS), by Takeda Science Foundation, and by Mochida Memorial Foundation for Medical and Pharmaceutical Research. |
| 出版者 |
|
|
出版者 |
American Society for Biochemistry and Molecular Biology |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 出版タイプ |
|
|
出版タイプ |
AO |
|
出版タイプResource |
http://purl.org/coar/version/c_b1a7d7d4d402bcce |
| 関連情報 |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
10.1074/mcp.RA119.001534 |
| 関連情報 |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.1074/mcp.RA119.001534 |
| 収録物識別子 |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
1535-9476 |
| 収録物識別子 |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
1535-9484 |
| 開始ページ |
|
|
開始ページ |
2044 |
| 書誌情報 |
Molecular & Cellular Proteomics
Molecular & Cellular Proteomics
巻 18,
号 10,
p. 2044-2057,
発行日 2019-08-02
|
| 旧ID |
48192 |
MCP_18_2044.pdf (2.6 MB)
