Direct interaction of the beta-domain of VHL tumor suppressor protein with the regulatory domain of atypical PKC isotypes

Biochem Biophys Res Commun. 1999 Sep 24;263(2):491-7. doi: 10.1006/bbrc.1999.1347.

Abstract

VHL tumor suppressor protein contains two domains, alpha and beta. The alpha-domain is involved in the formation of a large protein complex suggested to be involved in ubiquitin-mediated protein degradation. However, the role of the beta-domain, which may recognize the target proteins for protein degradation, remains unknown. Here we report that the beta-domain interacts directly with atypical PKC isotypes, PKCzeta and PKClambda. Further, the regulatory domain of aPKC is sufficient for this direct protein-protein interaction. Since aPKC isotypes have been implicated in the regulation of cell growth and apoptosis, these results suggest that aPKC isotypes are potential direct target of the VHL beta-domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cells, Cultured
  • Genes, Tumor Suppressor*
  • Humans
  • Isoenzymes / metabolism
  • Kidney / cytology
  • Ligases*
  • Molecular Sequence Data
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Precipitin Tests
  • Protein Binding
  • Protein Kinase C / genetics
  • Protein Kinase C / metabolism*
  • Proteins / genetics
  • Proteins / metabolism*
  • Recombinant Proteins / metabolism
  • Tumor Suppressor Proteins*
  • Ubiquitin-Protein Ligases*
  • Von Hippel-Lindau Tumor Suppressor Protein

Substances

  • Isoenzymes
  • Peptide Fragments
  • Proteins
  • Recombinant Proteins
  • Tumor Suppressor Proteins
  • Ubiquitin-Protein Ligases
  • Von Hippel-Lindau Tumor Suppressor Protein
  • protein kinase C gamma
  • protein kinase C zeta
  • Protein Kinase C
  • Ligases
  • VHL protein, human