Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN

Biochem Biophys Res Commun. 1997 May 29;234(3):621-5. doi: 10.1006/bbrc.1997.6669.


PKN is a serine/threonine protein kinase with a catalytic domain homologous to the protein kinase C family and unique N-terminal leucine zipper-like sequences. Using analyses with the yeast two-hybrid system and in vitro binding assay, we found that the regulatory domain of PKN interacted with vimentin. We then examined whether PKN would phosphorylate vimentin in vitro. Vimentin proved to be an excellent substrate for PKN, and the phosphorylation of vimentin by PKN occurred in the head domain with the result of a nearly complete inhibition of its filament formation in vitro. Similar results were also obtained with another type III intermediate filament protein, glial fibrillary acidic protein (GFAP). These results raise the possibility that PKN may regulate filament structures of vimentin and GFAP by domain-specific phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalysis
  • Glial Fibrillary Acidic Protein / metabolism*
  • Humans
  • Mice
  • Microscopy, Electron
  • Phosphorylation
  • Protein Kinase C
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein-Tyrosine Kinases / metabolism*
  • Recombinant Proteins / metabolism
  • Vimentin / metabolism*


  • Glial Fibrillary Acidic Protein
  • Recombinant Proteins
  • Vimentin
  • protein kinase N
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Protein Kinase C