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
Trong Nhat PhanWong, Ee LinSun, XiaoyanKim, GeunwoongJung, Seung HeeYoon, Chang NoYang, Beom-Seok
Issue Date
2013-09
Publisher
TAYLOR & FRANCIS LTD
Citation
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, v.77, no.9, pp.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.
Keywords
EXTRACELLULAR-MATRIX; COLLAGEN-BINDING; DDR1; ACTIVATION; GLYCAN; KINASE; ATHEROSCLEROSIS; IDENTIFICATION; PROLIFERATION; INFLAMMATION; EXTRACELLULAR-MATRIX; COLLAGEN-BINDING; DDR1; ACTIVATION; GLYCAN; KINASE; ATHEROSCLEROSIS; IDENTIFICATION; PROLIFERATION; INFLAMMATION; discoidin domain receptor; glucose; protein stability; N-glycosylation; asparagine
ISSN
0916-8451
URI
https://pubs.kist.re.kr/handle/201004/127718
DOI
10.1271/bbb.130351
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KIST Article > 2013
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