Arabidopsis thaliana KORRIGAN1 protein: N-glycan modification, localization, and
function in cellulose biosynthesis and osmotic stress responses
#MMPMID26039485
von Schaewen A
; Rips S
; Jeong IS
; Koiwa H
Plant Signal Behav
2015[]; 10
(5
): e1024397
PMID26039485
show ga
Plant cellulose biosynthesis is a complex process involving cellulose-synthase
complexes (CSCs) and various auxiliary factors essential for proper orientation
and crystallinity of cellulose microfibrils in the apoplast. Among them is
KORRIGAN1 (KOR1), a type-II membrane protein with multiple N-glycans within its
C-terminal cellulase domain. N-glycosylation of the cellulase domain was
important for KOR1 targeting to and retention within the trans-Golgi network
(TGN), and prevented accumulation of KOR1 at tonoplasts. The degree of successful
TGN localization of KOR1 agreed well with in vivo-complementation efficacy of the
rsw2-1 mutant, suggesting non-catalytic functions in the TGN. A dynamic
interaction network involving microtubules, CSCs, KOR1, and currently
unidentified glycoprotein component(s) likely determines stress-triggered
re-organization of cellulose biosynthesis and resumption of cell-wall growth
under stress.
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