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
- 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
- 판트롱낫; 이린옹; 선쇼앤; 김건웅; 정승희; 윤창노; 양범석
- discoidin domain receptor; glucose; protein stability; asparagine; N-glycosylation
- Issue Date
- Bioscience, biotechnology, and biochemistry
- VOL 77, NO 9, 1907-1916
- 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.
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