2014
DOI: 10.3389/fpls.2014.00363
|View full text |Cite
|
Sign up to set email alerts
|

Biological significance of complex N-glycans in plants and their impact on plant physiology

Abstract: Asparagine (N)-linked protein glycosylation is a ubiquitous co- and post-translational modification which can alter the biological function of proteins and consequently affects the development, growth, and physiology of organisms. Despite an increasing knowledge of N-glycan biosynthesis and processing, we still understand very little about the biological function of individual N-glycan structures in plants. In particular, the N-glycan-processing steps mediated by Golgi-resident enzymes create a structurally di… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
73
0
1

Year Published

2015
2015
2020
2020

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 91 publications
(75 citation statements)
references
References 75 publications
(102 reference statements)
1
73
0
1
Order By: Relevance
“…In contrast, Q361 is positioned at the end of an ␣ helix on the protein surface and located next to the amino acid sequence N362-G363-C364. This pattern follows the typical N-glycosylation sequence N-X-S/T/C of L-asparagine (N)-linked protein glycosylation, where X can be any amino acid except L-proline (45,46). Analysis of the PstrSTS2 amino acid sequence with the web server GlycoEP also identified N362 to be a potential site for N-glycosylation in this particular STS (47).…”
Section: Discussionmentioning
confidence: 99%
“…In contrast, Q361 is positioned at the end of an ␣ helix on the protein surface and located next to the amino acid sequence N362-G363-C364. This pattern follows the typical N-glycosylation sequence N-X-S/T/C of L-asparagine (N)-linked protein glycosylation, where X can be any amino acid except L-proline (45,46). Analysis of the PstrSTS2 amino acid sequence with the web server GlycoEP also identified N362 to be a potential site for N-glycosylation in this particular STS (47).…”
Section: Discussionmentioning
confidence: 99%
“…In particular, the initial (cotranslational) glycosylation steps in the ER play an important role in protein folding and quality control, including recognition by the ER-associated degradation pathway. The biology, significance, and detection of N-glycoproteins (the glycoproteome) in plants were recently extensively described and referenced (Song et al, , 2013Strasser, 2014). Since the vast majority of secretory proteins are glycosylated, many aspects of plant growth, development, metabolism, and (a)biotic responses are affected by N-glycosylation, including direct effects on enzyme functions.…”
Section: N-linked and O-linked Glycosylationmentioning
confidence: 99%
“…For instance, algae such as Codium fragile, Chondrus ocellatus, Sargassum piluliferum or Zostera marina contain only HMNGs, being devoid of CNGs (Yoshiie et al, 2012). Contrary to mammals, for which CNG defects are almost associated with diseases (congenital disorders of glycosylation), N-glycan processing in plant Golgi may be dispensable, although it is associated with disease under certain stress conditions (Strasser, 2014). In plants, free forms of N-glycans have also been detected at micromolar concentrations, during all stages of development (Maeda & Kimura, 2014).…”
Section: (B) Plant Mannosidesmentioning
confidence: 99%