Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan
Bibliographic Information
- Other Title
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- Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan*[S]
Abstract
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.
Journal
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- Molecular & Cellular Proteomics
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Molecular & Cellular Proteomics 18 (10), 2044-2057, 2019-08-02
American Society for Biochemistry and Molecular Biology
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Keywords
Details 詳細情報について
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- CRID
- 1050577740961120000
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- NII Article ID
- 120006731226
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- ISSN
- 15359476
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- IRDB
- Crossref
- CiNii Articles
- KAKEN