Plant protein glycosylation
Гликозилирование белков растений
2016-02-23
SCID: 54.1/nwq5bszc
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Lewis A-type structuresN-glycan biosynthesiscomplex N-glycansglycan-mediated quality controlplant protein glycosylation
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Abstract (AI)
Protein glycosylation is an essential co- and post-translational modification of secretory and membrane proteins in all eukaryotes. The initial steps of N-glycosylation and N-glycan processing are highly conserved between plants, mammals and yeast. In contrast, late N-glycan maturation steps in the Golgi differ significantly in plants giving rise to complex N-glycans with β1,2-linked xylose, core α1,3-linked fucose and Lewis A-type structures. While the essential role of N-glycan modifications on distinct mammalian glycoproteins is already well documented, we have only begun to decipher the biological function of this ubiquitous protein modification in different plant species. In this review, I focus on the biosynthesis and function of different protein N-linked glycans in plants. Special emphasis is given on glycan-mediated quality control processes in the ER and on the biological role of characteristic complex N-glycan structures.
Key Findings
1
Initial N-glycosylation steps and early N-glycan processing are highly conserved among plants, mammals, and yeast.
2
Plant Golgi maturation generates distinctive complex N-glycans containing β1,2-linked xylose, core α1,3-linked fucose, and Lewis A-type structures.
3
Plant N-glycans participate in endoplasmic-reticulum-mediated glycan quality-control processes.
4
The biological functions of N-glycan modifications remain less understood in plants than in mammals, despite their ubiquity.
5
The review emphasizes biosynthesis and biological roles of plant protein N-linked glycans, particularly characteristic complex structures.
Research Object
plant proteins and their N-linked glycans
Research Subject
the biosynthesis, maturation, quality-control functions, and biological roles of plant protein N-linked glycans, including characteristic complex N-glycan structures
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2016-02-23
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