DISSIMILAR PHORBOL ESTER BINDING-PROPERTIES OF THE INDIVIDUAL CYSTEINE-RICH MOTIFS OF PROTEIN-KINASE-D

Protein kinase D (PKD) is a serine/threonine kinase that binds phorbol esters in a phospholipid-dependent manner via a tandemly repeated cys teine-rich, zinc finger-like motif (the cysteine-rich domain, CRD), He re, we examined whether the individual cysteine-rich motifs of the CRD of PKD (referred to as cys1 and cys2) are functionally equivalent in mediating phorbol ester binding both in vivo and in vitro. Our results demonstrate that the cys1 and cys2 motifs of the CRD of PKD are funct ionally dissimilar, with the cys2 motif responsible for the majority o f [H-3]phorbol 12,13-dibutyrate (PDB) binding, both in vivo and in vit ro. (C) 1998 Federation of European Biochemical Societies.