Phosphorylation of hepatic insulin receptor by casein kinase 2.
Casein kinase 2 was able to phosphorylate the beta-subunit of hepatic insulin receptor in the presence of either ATP or GTP. Phosphorylation by casein kinase 2 was observed even in the absence of insulin, was inhibited by low heparin concentrations, and led to the incorporation of phosphate on serine and threonine residues. Casein kinase 2 phosphorylation of insulin receptor partially decreased its tyrosine kinase activity.
Grande
J
J
Departament de Bioquímica i Biologia Molecular (Facultat de Ciències), Universitat Autònoma de Barcelona, Spain.
Pérez
M
M
Itarte
E
E
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D047388:Casein Kinases; D002462:Cell Membrane / Q000032:analysis; D006160:Guanosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D006493:Heparin / Q000494:pharmacology; D008099:Liver / Q000032:analysis*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D051381:Rats; D011972:Receptor, Insulin / Q000378:metabolism*
D010769:Phosphothreonine; D010768:Phosphoserine; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D006493:Heparin; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin; D047388:Casein Kinases