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Unique substrate specificity and regulatory properties of PKC‐ε: a rationale for diversity
Author(s) -
Schaap Dick,
Parker Peter J.,
Bristol Andrew,
Kriz Ron,
Knopf John
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80160-7
Subject(s) - protein kinase c , substrate specificity , diversity (politics) , substrate (aquarium) , chemistry , biophysics , biochemistry , biology , kinase , enzyme , political science , ecology , law
PKC‐ε was isolated from a murine brain CDNA library. The clone, λ61PKC‐ε, 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‐ε, it was necessary to employ a synthetic peptide substrate based upon the pseudosubstrate site. Subsequent analysis demonstrated that PKC‐ε, while showing certain properties characteristic of the PKC family, has a quite distinct substrate specificity and is independent of Ca 2+ .