論文 - 詳細
| RRC ID | 37695 |
|---|---|
| 著者 | Sato Y, Isaji T, Tajiri M, Yoshida-Yamamoto S, Yoshinaka T, Somehara T, Fukuda T, Wada Y, Gu J. |
| タイトル | An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III. |
| ジャーナル | J Biol Chem |
| Abstract |
Recently we reported that N-glycans on the beta-propeller domain of the integrin alpha5 subunit (S-3,4,5) are essential for alpha5beta1 heterodimerization, expression, and cell adhesion. Herein to further investigate which N-glycosylation site is the most important for the biological function and regulation, we characterized the S-3,4,5 mutants in detail. We found that site-4 is a key site that can be specifically modified by N-acetylglucosaminyltransferase III (GnT-III). The introduction of bisecting GlcNAc into the S-3,4,5 mutant catalyzed by GnT-III decreased cell adhesion and migration on fibronectin, whereas overexpression of N-acetylglucosaminyltransferase V (GnT-V) promoted cell migration. The phenomenon is similar to previous observations that the functions of the wild-type alpha5 subunit were positively and negatively regulated by GnT-V and GnT-III, respectively, suggesting that the alpha5 subunit could be duplicated by the S-3,4,5 mutant. Interestingly GnT-III specifically modified the S-4,5 mutant but not the S-3,5 mutant. This result was confirmed by erythroagglutinating phytohemagglutinin lectin blot analysis. The reduction in cell adhesion was consistently observed in the S-4,5 mutant but not in the S-3,5 mutant cells. Furthermore mutation of site-4 alone resulted in a substantial decrease in erythroagglutinating phytohemagglutinin lectin staining and suppression of cell spread induced by GnT-III compared with that of either the site-3 single mutant or wild-type alpha5. These results, taken together, strongly suggest that N-glycosylation of site-4 on the alpha5 subunit is the most important site for its biological functions. To our knowledge, this is the first demonstration that site-specific modification of N-glycans by a glycosyltransferase results in functional regulation. |
| 巻・号 | 284(18) |
| ページ | 11873-81 |
| 公開日 | 2009-5-1 |
| DOI | 10.1074/jbc.M807660200 |
| PII | S0021-9258(20)58347-6 |
| PMID | 19276077 |
| PMC | PMC2673256 |
| MeSH | Animals CHO Cells Cell Adhesion / physiology Cell Movement / physiology* Cricetinae Cricetulus Dimerization Fibronectins Glycosylation HeLa Cells Humans Integrin alpha5 / genetics Integrin alpha5 / metabolism* Integrin alpha5beta1 / genetics Integrin alpha5beta1 / metabolism Mutation N-Acetylglucosaminyltransferases / genetics N-Acetylglucosaminyltransferases / metabolism* |
| IF | 4.238 |
| 引用数 | 37 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 2 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ヒト・動物細胞 | HeLa(RCB0007) |