Protein Glycosylation in Plant Development and Signal Transduction
A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Development and Morphogenesis".
Deadline for manuscript submissions: closed (30 November 2022) | Viewed by 348
Special Issue Editors
Interests: plant development; signaling; nucleocytoplasmic protein glycosylation; abiotic stress response; regulation of flowering time
Interests: plant N-glycosylation; transport and localization of N-glycosylation enzymes; protein transport signals; physiological function of N-glycans in plants
Special Issue Information
Dear Colleagues,
Protein glycosylation covers a group of heterogeneous co- and post-translational modifications with diverse roles in cell biology and development. The attachment of carbohydrates can affect protein structure, facilitate folding and stability, or mediate protein–protein interactions. Several types of protein glycosylation are found in different cellular compartments: Asparagine (N)-linked glycosylation takes place in the secretory pathway, where N-glycans of varying compositions are established. A subset of these N-glycans assist in folding as part of the glycan-dependent endoplasmic reticulum (ER) quality control, and play a role in the ER-associated degradation of glycoproteins. Many cell-wall proteins carry another type of extensive glycosylation. Serine- or threonine (O)-linked glycans (O-linked galactose, followed by complex arabinogalactan structures on hydroxyproline residues) are important for the formation and remodeling of functional cell walls, and also take part in cellular signaling. On the other hand, simple modification with O-linked monosaccharides is a very different type of protein glycosylation, which is found in a large number of nuclear and cytosolic proteins. This nucleocytoplasmic O-glycosylation plays an essential role within cells of all organisms. The molecular function of O-GlcNAcylation and O-fucosylation in plants is still not fully understood, but like other types of glycosylation, it affects protein structure and interactions, enabling cellular signaling during plant development. Additionally, a number of lectins are involved in signal transduction, by binding specifically to various types of carbohydrates.
For this Special Issue, we invite you to contribute articles highlighting the role of protein glycosylation in plant development and signal transduction—a research area where there is still a great deal to discover.
Dr. Doris Lucyshyn
Dr. Jennifer Schoberer
Guest Editors
Manuscript Submission Information
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Keywords
- protein glycosylation
- nucleotide sugar formation, interconversion and transporters
- N-glycosylation
- nucleocytoplasmic O-glycosylation
- GlcNAcylation and protein O-fucosylation
- arabinogalactan proteins
- hydroxyproline-rich glycoproteins
- plant lectins
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