PubMed:8662691 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":11,"end":18},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"}],"text":"The glut 1 glucose transporter interacts with calnexin and calreticulin.\nCalnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":72},"obj":"Sentence"},{"id":"T2","span":{"begin":73,"end":196},"obj":"Sentence"},{"id":"T3","span":{"begin":197,"end":323},"obj":"Sentence"},{"id":"T4","span":{"begin":324,"end":505},"obj":"Sentence"},{"id":"T5","span":{"begin":506,"end":647},"obj":"Sentence"},{"id":"T6","span":{"begin":648,"end":861},"obj":"Sentence"},{"id":"T7","span":{"begin":862,"end":1054},"obj":"Sentence"},{"id":"T8","span":{"begin":1055,"end":1148},"obj":"Sentence"},{"id":"T9","span":{"begin":1149,"end":1306},"obj":"Sentence"},{"id":"T10","span":{"begin":1307,"end":1411},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":72},"obj":"Sentence"},{"id":"T2","span":{"begin":73,"end":196},"obj":"Sentence"},{"id":"T3","span":{"begin":197,"end":323},"obj":"Sentence"},{"id":"T4","span":{"begin":324,"end":505},"obj":"Sentence"},{"id":"T5","span":{"begin":506,"end":647},"obj":"Sentence"},{"id":"T6","span":{"begin":648,"end":861},"obj":"Sentence"},{"id":"T7","span":{"begin":862,"end":1054},"obj":"Sentence"},{"id":"T8","span":{"begin":1055,"end":1148},"obj":"Sentence"},{"id":"T9","span":{"begin":1149,"end":1306},"obj":"Sentence"},{"id":"T10","span":{"begin":1307,"end":1411},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The glut 1 glucose transporter interacts with calnexin and calreticulin.\nCalnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":11,"end":18},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"The glut 1 glucose transporter interacts with calnexin and calreticulin.\nCalnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":4,"end":10},"obj":"protein"},{"id":"T2","span":{"begin":46,"end":54},"obj":"protein"},{"id":"T3","span":{"begin":59,"end":71},"obj":"protein"},{"id":"T4","span":{"begin":73,"end":81},"obj":"protein"},{"id":"T5","span":{"begin":286,"end":294},"obj":"protein"},{"id":"T6","span":{"begin":382,"end":388},"obj":"protein"},{"id":"T7","span":{"begin":390,"end":395},"obj":"protein"},{"id":"T8","span":{"begin":628,"end":633},"obj":"protein"},{"id":"T9","span":{"begin":638,"end":646},"obj":"protein"},{"id":"T10","span":{"begin":759,"end":764},"obj":"protein"},{"id":"T11","span":{"begin":814,"end":820},"obj":"protein"},{"id":"T12","span":{"begin":822,"end":849},"obj":"protein"},{"id":"T13","span":{"begin":871,"end":876},"obj":"protein"},{"id":"T14","span":{"begin":877,"end":885},"obj":"protein"},{"id":"T15","span":{"begin":894,"end":899},"obj":"protein"},{"id":"T16","span":{"begin":900,"end":906},"obj":"protein"},{"id":"T17","span":{"begin":1000,"end":1005},"obj":"protein"},{"id":"T18","span":{"begin":1032,"end":1040},"obj":"protein"},{"id":"T19","span":{"begin":1057,"end":1062},"obj":"protein"},{"id":"T20","span":{"begin":1129,"end":1137},"obj":"protein"},{"id":"T21","span":{"begin":1141,"end":1147},"obj":"protein"},{"id":"T22","span":{"begin":1149,"end":1161},"obj":"protein"},{"id":"T23","span":{"begin":1188,"end":1196},"obj":"protein"},{"id":"T24","span":{"begin":1230,"end":1235},"obj":"protein"},{"id":"T25","span":{"begin":1337,"end":1345},"obj":"protein"},{"id":"T26","span":{"begin":1350,"end":1362},"obj":"protein"},{"id":"T27","span":{"begin":1368,"end":1374},"obj":"protein"}],"text":"The glut 1 glucose transporter interacts with calnexin and calreticulin.\nCalnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":97,"end":105},"obj":"Body_part"},{"id":"T4","span":{"begin":186,"end":195},"obj":"Body_part"},{"id":"T5","span":{"begin":360,"end":368},"obj":"Body_part"},{"id":"T8","span":{"begin":425,"end":437},"obj":"Body_part"},{"id":"T9","span":{"begin":476,"end":482},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A7","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL_0000558"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0003674"}],"text":"The glut 1 glucose transporter interacts with calnexin and calreticulin.\nCalnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":425,"end":437},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000558"}],"text":"The glut 1 glucose transporter interacts with calnexin and calreticulin.\nCalnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner."}