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10.1080/15592324.2015.1024397

http://scihub22266oqcxt.onion/10.1080/15592324.2015.1024397
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suck abstract from ncbi


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pmid26039485      Plant+Signal+Behav 2015 ; 10 (5): ä
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  • 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[May]; 10 (5): ä PMID26039485show 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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