Academic Journal
Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A)
| العنوان: | Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A) |
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| المؤلفون: | Nagae, Masamichi, Hirata, Tetsuya, Tateno, Hiroaki, Mishra, Sushil K., Manabe, Noriyoshi, Osada, Naoko, Tokoro, Yuko, Yamaguchi, Yoshiki, Doerksen, Robert J., Shimizu, Toshiyuki, Kizuka, Yasuhiko |
| المساهمون: | MEXT | Japan Society for the Promotion of Science, U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences, MEXT | Japan Science and Technology Agency, Takeda Science Foundation, Tokyo Biochemical Research Foundation |
| المصدر: | Communications Biology ; volume 5, issue 1 ; ISSN 2399-3642 |
| بيانات النشر: | Springer Science and Business Media LLC |
| سنة النشر: | 2022 |
| الوصف: | N -Glycosylation is a common post-translational modification, and the number of GlcNAc branches in N -glycans impacts glycoprotein functions. N -Acetylglucosaminyltransferase-IVa (GnT-IVa, also designated as MGAT4A) forms a β1-4 GlcNAc branch on the α1-3 mannose arm in N -glycans. Downregulation or loss of GnT-IVa causes diabetic phenotypes by dysregulating glucose transporter-2 in pancreatic β-cells. Despite the physiological importance of GnT-IVa, its structure and catalytic mechanism are poorly understood. Here, we identify the lectin domain in mouse GnT-IVa’s C-terminal region. The crystal structure of the lectin domain shows structural similarity to a bacterial GlcNAc-binding lectin. Comprehensive glycan binding assay using 157 glycans and solution NMR reveal that the GnT-IVa lectin domain selectively interacts with the product N -glycans having a β1-4 GlcNAc branch. Point mutation of the residue critical to sugar recognition impairs the enzymatic activity, suggesting that the lectin domain is a regulatory subunit for efficient catalytic reaction. Our findings provide insights into how branching structures of N -glycans are biosynthesized. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| DOI: | 10.1038/s42003-022-03661-w |
| الاتاحة: | http://dx.doi.org/10.1038/s42003-022-03661-w https://www.nature.com/articles/s42003-022-03661-w.pdf https://www.nature.com/articles/s42003-022-03661-w |
| Rights: | https://creativecommons.org/licenses/by/4.0 ; https://creativecommons.org/licenses/by/4.0 |
| رقم الانضمام: | edsbas.C7FDE0F5 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1038/s42003-022-03661-w |
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