title: Dissociation of the hepatic insulin receptor favours its phosphorylation by casein kinase 2.
abstract: The alpha beta heterodimeric form of untreated hepatic insulin receptor was a substrate for casein kinase 2, whereas the alpha 2 beta 2 heterotetramer was not. On the contrary, autophosphorylation was detected only in the heterotetramer. Dissociation of the receptor by treatment with dithiothreitol decreased its autophosphorylation but favoured phosphorylation of its beta-subunit by casein kinase 2.
authors.affiliation: Department de Bioquímica i Biologia molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Trujillo
authors.forename: M
authors.initials: M
authors.lastname: Jose
authors.forename: M
authors.initials: M
authors.lastname: Plana
authors.forename: E
authors.initials: E
authors.lastname: Molina
authors.forename: E
authors.initials: E
authors.lastname: Itarte
mesh_terms: D000818:Animals; D047388:Casein Kinases; D004229:Dithiothreitol / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008099:Liver / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011972:Receptor, Insulin / Q000378:metabolism*
chemical_list: D011494:Protein Kinases; D011972:Receptor, Insulin; D047388:Casein Kinases; D004229:Dithiothreitol