{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pedersen NB"],"funding":["Canadian Institutes of Health Research"],"pagination":["17312-24"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4067166"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["289(25)"],"pubmed_abstract":["The low density lipoprotein receptor (LDLR) is crucial for cholesterol homeostasis and deficiency in LDLR functions cause hypercholesterolemia. LDLR is a type I transmembrane protein that requires O-glycosylation for stable expression at the cell surface. It has previously been suggested that LDLR O-glycosylation is found N-terminal to the juxtamembrane region. Recently we identified O-glycosylation sites in the linker regions between the characteristic LDLR class A repeats in several LDLR-related receptors using the \"SimpleCell\" O-glycoproteome shotgun strategy. Herein, we have systematically characterized O-glycosylation sites on recombinant LDLR shed from HEK293 SimpleCells and CHO wild-type cells. We find that the short linker regions between LDLR class A repeats contain an evolutionar"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Low density lipoprotein receptor class A repeats are O-glycosylated in linker regions."],"pmcid":["PMC4067166"],"funding_grant_id":["102741"],"pubmed_authors":["Schjoldager KT","Madsen TD","Yang Z","Halim A","Seidah NG","Wang S","Bennett EP","Clausen H","Narimatsu Y","Pedersen NB","Levery SB"],"additional_accession":[]},"is_claimable":false,"name":"Low density lipoprotein receptor class A repeats are O-glycosylated in linker regions.","description":"The low density lipoprotein receptor (LDLR) is crucial for cholesterol homeostasis and deficiency in LDLR functions cause hypercholesterolemia. LDLR is a type I transmembrane protein that requires O-glycosylation for stable expression at the cell surface. It has previously been suggested that LDLR O-glycosylation is found N-terminal to the juxtamembrane region. Recently we identified O-glycosylation sites in the linker regions between the characteristic LDLR class A repeats in several LDLR-related receptors using the \"SimpleCell\" O-glycoproteome shotgun strategy. Herein, we have systematically characterized O-glycosylation sites on recombinant LDLR shed from HEK293 SimpleCells and CHO wild-type cells. We find that the short linker regions between LDLR class A repeats contain an evolutionar","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jun","modification":"2026-04-17T15:08:17.901Z","creation":"2019-03-27T01:30:41Z"},"accession":"S-EPMC4067166","cross_references":{"pubmed":["24798328"],"doi":["10.1074/jbc.m113.545053","10.1074/jbc.M113.545053"]}}