Phosphorylation of neurofibromatosis type 1 gene product (neurofibromin) by cAMP-dependent protein kinase

Ichiro Izawa, Norihiko Tamaki, Hideyuki Saya

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

The critical function of the neurofibromatosis type 1 (NF1) gene product (neurofibromin) is not well defined except that neurofibromin has homology with a family of the GTPase-activating proteins (GAPs). In this study, we confirmed that neurofibromin is constitutively phosphorylated and detected kinase activities which specifically phosphorylate the cystein/serine-rich domain and the C-terminal domain of the neurofibromin in cell lysate. In vitro and in-gel kinase assays strongly indicated that cAMP-dependent protein kinase (PKA) is a candidate for the neurofibromin kinase. The biological significance of the phosphorylation of neurofibromin is unclear at present, but we speculate that neurofibromin plays a crucial role in cellular function since it links the two major cellular pathways which are the GAP-ras and PKA-associated signals.

Original languageEnglish
Pages (from-to)53-59
Number of pages7
JournalFEBS Letters
Volume382
Issue number1-2
DOIs
Publication statusPublished - 1996 Mar 11
Externally publishedYes

Keywords

  • Neurofibromatosis type 1 (NF1)
  • Neurofibromin
  • Phosphorylation
  • cAMP-dependent protein kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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