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

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Signal Transduction Mechanisms

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 are in 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 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 (Cl) domain in PKC.

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Aitken, A. et al. (1995). Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C. In: Barnes, J.A., Coore, H.G., Mohammed, A.H., Sharma, R.K. (eds) Signal Transduction Mechanisms. Developments in Molecular and Cellular Biochemistry, vol 15. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2015-3_5

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  • DOI: https://doi.org/10.1007/978-1-4615-2015-3_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5833-6

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