Mechanism of Inhibition of Protein Kinase C by 14-3-3 Isoforms. 14-3-3 Isoforms Do Not Have Phospholipase A2 Activity

Overview

Journal Biochem J

Specialty Biochemistry

Date 1994 May 1

PMID 8192676

Citations 25

Authors

K Robinson

D Jones

Y Patel

H Martin

J Madrazo

S Martin

S Howell

M Elmore

M J Finnen

A Aitken

Affiliations

Soon will be listed here.

Abstract

The ability of individual members of the 14-3-3 protein family to inhibit protein kinase C (PKC) has been studied by using a synthetic peptide based on the specific 80 kDa substrate for PKC (MARCKS protein) in two different assay systems. Recombinant 14-3-3 and isoforms renatured by a novel method after separation by reverse-phase h.p.l.c. were studied. The detailed effects of diacylglycerol and the phorbol ester phorbol 12-myristate 13-acetate on the inhibition were also investigated. This suggests that one of the sites of interaction of 14-3-3 may be the cysteine-rich (C1) domain in PKC. Since a region in secreted phospholipase A2 (PLA2) shares similarity with this domain, the ability of 14-3-3 to interact with mammalian PLA2 was studied. Cytosolic PLA2 has some similarity to the C2 region of PKC, and the effect of 14-3-3 on this class of PLA2 was also analysed. In contrast with a previous report, no PLA2 activity was found in brain 14-3-3, nor in any of the recombinant proteins tested. These include zeta 14-3-3 isoform, on which the original observation was made.

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