Defective Ca(2+) binding in a conserved binding site causes incomplete N-glycan processing and endoplasmic reticulum trapping of discoidin domain receptors

Title
Defective Ca(2+) binding in a conserved binding site causes incomplete N-glycan processing and endoplasmic reticulum trapping of discoidin domain receptors
Authors
판트롱낫이린옹박선영김해종양범석
Keywords
Calcium signaling; Discoidin domain receptor; posttranslational modification; endoplasmic reticulum
Issue Date
2015-04
Publisher
Bioscience, biotechnology, and biochemistry
Citation
VOL 79, NO 4, 574-580
Abstract
An X-ray crystallographic study has suggested that vertebrate discoidin domain receptors (DDRs) have a conserved Ca2+ binding site. DDR1 and DDR2 transfected in HEK293 cells were expressed mainly as 120 and 130 kDa forms, respectively, as they are sufficiently N-glycosylated. However, both of them showed the molecular weight of 110 kDa predominantly in the cells cultured with Ca2+- depleted media. DDR2-carrying D234A mutation at the conserved Ca2+-binding site expressed the 110 kDa form dominantly even in normal culture condition. DDR2 becomes 100 kDa form in glucosedepleted culture condition and its molecular weight increases up to 130 kDa with re-feeding glucose. However, in the mutant DDR2, the increase came to a halt at 110 kDa. The 110 kDa form had premature N-glycosyl carbohydrates and located predominantly within the endoplasmic reticulum. These results suggest that DDRs require Ca2+-binding to complete their N-glycan processing and generate the form targeted to cell membrane.
URI
http://pubs.kist.re.kr/handle/201004/50633
ISSN
09168451
Appears in Collections:
KIST Publication > Article
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