Phosphorylation of neurofibromin by cAMP-dependent protein kinase is regulated via a cellular association of NG,NG-dimethylarginine dimethylaminohydrolase

Hiroshi Tokuo, Shunji Yunoue, Liping Feng, Masumi Kimoto, Hideaki Tsuji, Tomomichi Ono, Hideyuki Saya, Norie Araki

研究成果: Article査読

43 被引用数 (Scopus)

抄録

The neurofibromatosis type 1 (NF1) tumor suppressor (neurofibromin) is thought to play crucial roles in cellular Ras- and cAMP-dependent kinase (PKA)-associated signals. In this study, we identified a cellular neurofibromin-associating protein, NG,NG-dimethylarginine dimethylaminohydrolase (DDAH) that is known as a cellular NO/NOS regulator. The interaction of DDAH was mainly directed to the C-terminal domain (CTD) and to the cysteine/serine-rich domain (CSRD) of neurofibromin, coinciding with the regions containing specific PKA phosphorylation sites. DDAH increased PKA phosphorylation of native neurofibromin in a dose-dependent manner, especially affecting the phosphorylation of CSRD. These findings suggest that the PKA accessibility of neurofibromin was regulated via DDAH interaction, and this regulation may modulate the cellular function of neurofibromin that is implicated in NF1-related pathogenesis.

本文言語English
ページ(範囲)48-53
ページ数6
ジャーナルFEBS Letters
494
1-2
DOI
出版ステータスPublished - 06-04-2001
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

フィンガープリント

「Phosphorylation of neurofibromin by cAMP-dependent protein kinase is regulated via a cellular association of N<sup>G</sup>,N<sup>G</sup>-dimethylarginine dimethylaminohydrolase」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル