Unique substrate specificity and regulatory properties of PKC‐ε: a rationale for diversity

FEBS Letters

Bristol, Andrew¹  Knopf, John¹  Parker, Peter J.²  Schaap, Dick²  Kriz, Ron¹ 

[1] Genetics Institute, Cambridge, MA, USA;Ludwig Institute for Cancer Research, London, England

关键词: Protein kinase C;    Substrate specificity;    Ca2+;    Phosphorylation;    Gene family;    Protein kinase C-ε;   

DOI  :  10.1016/0014-5793(89)80160-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺.

【 授权许可】

Unknown