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Phosphorylation of neurofibromatosis type 1 gene product (neurofibromin) by cAMP‐dependent protein kinase
Author(s) -
Izawa Ichiro,
Tamaki Norihiko,
Saya Hideyuki
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00137-8
Subject(s) - neurofibromin 1 , cyclin dependent kinase 9 , microbiology and biotechnology , gene product , phosphorylation , protein kinase a , protein kinase domain , kinase , mitogen activated protein kinase kinase , map kinase kinase kinase , biology , map2k7 , neurofibromatosis , cyclin dependent kinase 2 , chemistry , gene , biochemistry , genetics , gene expression , mutant
The critical function of the neurofibromatosis type 1 NF 1) gene product (neurofabromin) is not well defined except that neurofibromin has homology with a family of the GTPase‐activating proteins (GAPs). In this study, we confirmed that neuofibromin is constitutively phosphorylated and detected kinase activities which specifically phosphorylated the cysteine/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 for the phosphorylation of neuofibromin 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‐rins and PKA‐associated signals.