Substrate specificities of insulin and epidermal growth factor receptor kinases.
The abilities of insulin and EGF stimulated protein kinases to phosphorylate a series of exogenous substrates were compared using wheat germ lectin purified preparations of solubilized rat liver membranes. Three different kinds of substrates were found: substrates phosphorylated primarily by insulin stimulated kinase, substrates phosphorylated primarily by EGF stimulated kinase and substrates phosphorylated by both kinases to a similar extent. These results indicate that the insulin and the EGF receptor kinase have different, but overlapping, substrate specificities. In vivo, phosphorylation of cellular proteins by various hormone receptor kinases may be part of the signal transmission process for actions of the hormones. Different substrate specificities of kinases of different hormone receptors may therefore represent an important mechanism to preserve the specificity of the hormonal signal at the post receptor level.
Klein
H H
HH
Freidenberg
G R
GR
Cordera
R
R
Olefsky
J M
JM
D000804:Angiotensin II / Q000378:metabolism; D000818:Animals; D002364:Caseins / Q000378:metabolism; D066246:ErbB Receptors; D006657:Histones / Q000378:metabolism; D036341:Intercellular Signaling Peptides and Proteins; D008099:Liver / Q000201:enzymology; D008297:Male; D009842:Oligopeptides / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011972:Receptor, Insulin / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013379:Substrate Specificity
D002364:Caseins; D006657:Histones; D036341:Intercellular Signaling Peptides and Proteins; D009842:Oligopeptides; D010455:Peptides; D011956:Receptors, Cell Surface; C040475:Src peptide; D000804:Angiotensin II; C027606:L-glutamic acid-L-tyrosine copolymer; D011494:Protein Kinases; D066246:ErbB Receptors; D011972:Receptor, Insulin