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The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C.

The atypical PKCs are involved in a number of important cellular functions, including cell proliferation. We report here that the product of the par-4 gene specifically interacts with the regulatory domains of zeta PKC and lambda/LPKC, which dramatically inhibits their enzymatic activity. This is particularly challenging, because expression of par-4 has been shown to correlate with growth inhibition and apoptosis. Results are shown here demonstrating that the expression of par-4 in NIH-3T3 cells induces morphological changes typical of apoptosis, which are abrogated by cotransfection of either wild-type zeta PKC or lambda/LPKC, but not by their respective kinase-inactive mutants. These findings support a role for the atypical PKC subspecies in the control of cell growth and survival.

Pubmed ID: 8797824


  • Díaz-Meco MT
  • Municio MM
  • Frutos S
  • Sanchez P
  • Lozano J
  • Sanz L
  • Moscat J



Publication Data

September 6, 1996

Associated Grants


Mesh Terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Bacterial Proteins
  • Base Sequence
  • Carrier Proteins
  • Cell Line
  • Cercopithecus aethiops
  • Cloning, Molecular
  • Enzyme Inhibitors
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Isoenzymes
  • Mice
  • Molecular Sequence Data
  • Promoter Regions, Genetic
  • Protein Binding
  • Protein Kinase C
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-mos
  • Proto-Oncogene Proteins c-raf
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases
  • Zinc Fingers