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
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
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. N-glycosylation, , -, -, site
- 3. N-glycosylation, , -, -, site
- 3. N-glycosylation, , -, -, sites
- 5. N-glycosylation, , -, -, site
- 5. site, , -, the glucose supply, site
Output(Part-Of) (sent_index,
protein,
site):
- 3. DDR1, asparagine 211
- 3. DDR1, site
- 3. DDR2, asparagine 213
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):