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- Title
Multiple N-Glycans Cooperate in the Subcellular Targeting and Functioning of Arabidopsis KORRIGAN1.
- Authors
Rips, Stephan; Bentley, Nolan; Jeong, In Sil; Welch, Justin L.; Schaewen, Antje von; Koiwa, Hisashi
- Abstract
Arabidopsis thaliana KORRIGAN1 (KOR1) is an integral membrane endo-β1,4-glucanase in the trans -Golgi network and plasma membrane that is essential for cellulose biosynthesis. The extracellular domain of KOR1 contains eight N -glycosylation sites, N1 to N8, of which only N3 to N7 are highly conserved. Genetic evidence indicated that cellular defects in attachment and maturation of these N -glycans affect KOR1 function in vivo, whereas the manner by which N -glycans modulate KOR1 function remained obscure. Site-directed mutagenesis analysis of green fluorescent protein (GFP)-KOR1 expressed from its native regulatory sequences established that all eight N -glycosylation sites (N1 to N8) are used in the wild type, whereas stt3a-2 cells could only inefficiently add N -glycans to less conserved sites. GFP-KOR1 variants with a single N -glycan at nonconserved sites were less effective than those with one at a highly conserved site in rescuing the root growth phenotype of rsw2-1 (kor1 allele). When functionally compromised, GFP-KOR1 tended to accumulate at the tonoplast. GFP-KOR1Δall (without any N -glycan) exhibited partial complementation of rsw2-1 ; however, root growth of this line was still negatively affected by the absence of complex-type N -glycan modifications in the host plants. These results suggest that one or several additional factor(s) carrying complex N -glycans cooperate(s) with KOR1 in trans to grant proper targeting/functioning in plant cells.
- Subjects
GREEN fluorescent protein; ROOT growth; SITE-specific mutagenesis; ARABIDOPSIS; HOST plants
- Publication
Plant Cell, 2014, Vol 26, Issue 9, p3792
- ISSN
1040-4651
- Publication type
Article
- DOI
10.1105/tpc.114.129718