A phorbol ester‐responsive PKC‐ζ generated by fusion with the regulatory domain of PKC‐δ

FEBS Letters

Parker, Peter J.²  Goode, Nigel T.¹ 

[1] Department of Veterinary Basic Sciences, The Royal Veterinary College, Royal College Street, London NW1 OTU, UK;Protein Phosphorylation Laboratory, Imperial Cancer Research Fund Laboratories, PO Box 123, London WC2A 3PX, UK

关键词: Isotype regulation;    Phosphorylation;    Protein kinase C;    Protein kinase C-ζ;    Substrate specificity;    Schizosaccharomyces pombe;    PK-C;    protein kinase C;    PSS;    pseudosubstrate site;    TPA;    12-O-tetradecanoylphorbol 13-acetate;    PS;    phosphatidylserine;   

DOI  :  10.1016/0014-5793(94)80190-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A hybrid molecule generated by fusing the regulatory domain of PKC-δ with the catalytic domain of PKC-ζ is, like PKC-δ but unlike PKC-ζ, a phorbol ester-dependent enzyme. However, the substrate specificity of this hybrid resembles that of PKC-ζ. Expression of mammalian PKC-δ, but not PKC-ζ, m the fission yeast Schizosaccharomyces pombe causes growth retardation and phorbol esters amplify the PKC-δ phenotype without affecting that of PKC-ζ (Goode et al., submitted). The chimaeric molecule also inhibited growth and this effect was phorbol-ester dependent. Both the hybrid and PKC-δ holoenzyme, in contrast to PKC-ζ, down-regulate upon prolonged exposure to phorbol esters in vivo. Thus, this hybrid retains the regulatory properties conferred by PKC-δ but the catalytic properties of PKC-ζ. This regulatable chimaeric molecule will be useful in assessing the function of PKC-ζ.

【 授权许可】

Unknown