Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C - PubMed (original) (raw)

. 1995 Aug-Sep:149-150:41-9.

doi: 10.1007/BF01076562.

Affiliations

• PMID: 8569748
• DOI: 10.1007/BF01076562

Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C

A Aitken et al. Mol Cell Biochem. 1995 Aug-Sep.

Abstract

This report compares the ability of individual members of the 14-3-3 protein family to inhibit particular protein kinase C (PKC) isoforms. We also show that two of these 14-3-3 isoforms (alpha and delta) specific to mammalian and avian brain are in vivo post-translationally modified forms of beta and zeta respectively. The presence of this modification enhances the activity of 14-3-3 as an inhibitor of protein kinase C nearly two fold. A method for analysing isoforms of 14-3-3 on acid-urea gels is also described. This permits the complete separation of all major isoforms and their unequivocal identification by a range of isoform specific antisera. The activity of recombinant 14-3-3 and isoforms renatured by a novel method after separation by reverse phase HPLC are compared. The effects of diacylglycerol and the phorbol ester, PMA (phorbol 1 2-myristate 13 acetate) on the inhibition suggest that one of the sites of interaction of 14-3-3 may be the cysteine-rich (C1) domain in PKC.

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