Low Stability and a Conserved N-Glycosylation Site Are Associated with Regulation of the Discoidin Domain Receptor Family by Glucose via Post-Translational N-Glycosylation

Title
Low Stability and a Conserved N-Glycosylation Site Are Associated with Regulation of the Discoidin Domain Receptor Family by Glucose via Post-Translational N-Glycosylation
Authors
판트롱낫이린옹선쇼앤김건웅정승희윤창노양범석
Keywords
discoidin domain receptor; glucose; protein stability; asparagine; N-glycosylation
Issue Date
2013-09
Publisher
Bioscience, biotechnology, and biochemistry
Citation
VOL 77, NO 9, 1907-1916
Abstract
Cell-surface expression of the discoidin domain receptor (DDR) tyrosine kinase family in high molecular mass form was controlled sensitively by the glucose concentration through a post-translational N-glycosylation process. Cycloheximide time-course experiments revealed that the high-molecular-mass forms of DDR1 and DDR2 were significantly less stable than control receptor tyrosine kinases. Site-directed mutational analysis of the consensus N-glycosylation sites of the DDRs revealed that mutations of asparagine 213 of DDR2 and asparagine 211 of DDR1, a conserved N-glycosylation site among vertebrate DDRs, inhibited the generation of the high-molecular-mass isoform. Taken together, these results suggest a mechanism to control the activity of the DDR family by regulating its cell-surface expression. Due to low stability, the steady-state population of functional DDR proteins in the cell surface depends sensitively on its maturation process via post-translational N-glycosylation, which is controlled by the glucose supply and the presence of a conserved N-glycosylation site.
URI
http://pubs.kist.re.kr/handle/201004/46304
ISSN
09168451
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KIST Publication > Article
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