Dissociation of the hepatic insulin receptor favours its phosphorylation by casein kinase 2.
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.
Trujillo
R
R
Department de Bioquímica i Biologia molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
Jose
M
M
Plana
M
M
Molina
E
E
Itarte
E
E
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*
D011494:Protein Kinases; D011972:Receptor, Insulin; D047388:Casein Kinases; D004229:Dithiothreitol