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

研究成果: ジャーナルへの寄稿学術論文査読

64 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)621-625
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
234
3
DOI
出版ステータス出版済み - 29-05-1997
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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