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 (α and δ) specific to mammalian and avian brain arein vivo post-translationally modified forms of β and ζ 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 12-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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Aitken, A., Howell, S., Jones, D. et al. Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C. Mol Cell Biochem 149, 41–49 (1995). https://doi.org/10.1007/BF01076562
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DOI: https://doi.org/10.1007/BF01076562