| First Author | Schaap D | Year | 1989 |
| Journal | FEBS Lett | Volume | 243 |
| Issue | 2 | Pages | 351-7 |
| PubMed ID | 2917656 | Mgi Jnum | J:49534 |
| Mgi Id | MGI:1278308 | Doi | 10.1016/0014-5793(89)80160-7 |
| Citation | Schaap D, et al. (1989) Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity. FEBS Lett 243(2):351-7 |
| abstractText | 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+. |
