Trong-Nhat Phan Wong, Ee Lin Park, Sun Young Kim, Hae Jong Yang, Beom-Seok 2024-01-20T07:04:59Z 2024-01-20T07:04:59Z 2021-09-05 2015-04-03 0916-8451 https://pubs.kist.re.kr/handle/201004/125555 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 130kDa forms, respectively, as they are sufficiently N-glycosylated. However, both of them showed the molecular weight of 110kDa predominantly in the cells cultured with Ca2+-depleted media. DDR2-carrying D234A mutation at the conserved Ca2+-binding site expressed the 110kDa form dominantly even in normal culture condition. DDR2 becomes 100kDa form in glucose-depleted culture condition and its molecular weight increases up to 130kDa with re-feeding glucose. However, in the mutant DDR2, the increase came to a halt at 110kDa. The 110kDa 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. English TAYLOR & FRANCIS LTD DDR2 PROLIFERATION INFLAMMATION ACTIVATION MUTATIONS KINASES FAMILY MATRIX GENE Defective Ca2+ binding in a conserved binding site causes incomplete N-glycan processing and endoplasmic reticulum trapping of discoidin domain receptors Article 10.1080/09168451.2014.987208 1 BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, v.79, no.4, pp.574 - 580 BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 79 4 574 580 scie scopus 000353479000007 2-s2.0-84927620683 Biochemistry & Molecular Biology Biotechnology & Applied Microbiology Chemistry, Applied Food Science & Technology Biochemistry & Molecular Biology Biotechnology & Applied Microbiology Chemistry Food Science & Technology Article DDR2 PROLIFERATION INFLAMMATION ACTIVATION MUTATIONS KINASES FAMILY MATRIX GENE calcium binding posttranslational modification endoplasmic reticulum discoidin domain receptor