Dissimilar phorbol ester binding properties of the individual cysteine-rich motifs of protein kinase D

FEBS Lett. 1998 Oct 16;437(1-2):19-23. doi: 10.1016/s0014-5793(98)01189-2.

Abstract

Protein kinase D (PKD) is a serine/threonine kinase that binds phorbol esters in a phospholipid-dependent manner via a tandemly repeated cysteine-rich, zinc finger-like motif (the cysteine-rich domain, CRD). Here, we examined whether the individual cysteine-rich motifs of the CRD of PKD (referred to as cysl and cys2) are functionally equivalent in mediating phorbol ester binding both in vivo and in vitro. Our results demonstrate that the cysl and cys2 motifs of the CRD of PKD are functionally dissimilar, with the cys2 motif responsible for the majority of [3H]phorbol 12,13-dibutyrate (PDB) binding, both in vivo and in vitro.

MeSH terms

  • Animals
  • COS Cells
  • Cysteine
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism
  • Mutagenesis, Site-Directed
  • Phorbol 12,13-Dibutyrate / metabolism
  • Phorbol Esters / metabolism*
  • Protein Kinase C / chemistry
  • Protein Kinase C / metabolism*
  • Recombinant Proteins / metabolism
  • Transfection

Substances

  • Phorbol Esters
  • Recombinant Proteins
  • Phorbol 12,13-Dibutyrate
  • Glutathione Transferase
  • protein kinase D
  • Protein Kinase C
  • Cysteine