Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity.
PKC-epsilon was isolated from a murine brain cDNA library. The clone, lambda 61PKC-epsilon, encoded a polypeptide of 737 amino acids that is homologous to other PKCs. Northern analysis showed that the 7 kb mRNA for this cDNA is widely expressed. The protein when expressed in COS-1 cells displayed phorbol ester-binding activity. However in order to detect the kinase activity of PKC-epsilon, it was necessary to employ a synthetic peptide substrate based upon the pseudosubstrate site. Subsequent analysis demonstrated that PKC-epsilon, while showing certain properties characteristic of the PKC family, has a quite distinct substrate specificity and is independent of Ca2+.
Schaap
D
D
Ludwig Institute for Cancer Research, London, England.
Parker
P J
PJ
Bristol
A
A
Kriz
R
R
Knopf
J
J
D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D001921:Brain / Q000201:enzymology; D002852:Chromatography, Ion Exchange; D004247:DNA / Q000032:analysis; D051379:Mice; D008969:Molecular Sequence Data; D015240:Phorbol 12,13-Dibutyrate / Q000378:metabolism; D011485:Protein Binding; D011493:Protein Kinase C / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D014162:Transfection
D015240:Phorbol 12,13-Dibutyrate; D004247:DNA; D011493:Protein Kinase C