Evidence for phosphorylation of actin by the insulin receptor-associated protein kinase from human placenta.
A purified preparation of rabbit muscle actin (43-kDa protein) is phosphorylated at tyrosine residues when incubated with solubilized insulin receptor from human placenta. Phosphorylation of the 95-kDa receptor subunit and of 43-kDa protein is stimulated by insulin and vanadate, respectively; however, the mode of action of the two agents is distinguishable.
D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D010766:Phosphorylation; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011972:Receptor, Insulin / Q000302:isolation & purification / Q000378:metabolism*
D000199:Actins; D011494:Protein Kinases; D011972:Receptor, Insulin