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

Kaori Matsuzawa, Hidetaka Kosako, Naoyuki Inagaki, Hideki Shibata, Hideyuki Mukai, Yoshitaka Ono, Mutsuki Amano, Kozo Kaibuchi, Yoshiharu Matsuura, Ichiro Azuma, Masaki Inagaki

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)621-625
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 29-05-1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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