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

Ichiro Izawa, Norihiko Tamaki, Hideyuki Saya

Research output: Contribution to journalArticle

53 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

Fingerprint

Neurofibromin 1
Phosphorylation
Cyclic AMP-Dependent Protein Kinases
GTPase-Activating Proteins
Phosphotransferases
ras Proteins
Protein Kinases
Serine
Assays
Gels
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of neurofibromatosis type 1 gene product (neurofibromin) by cAMP-dependent protein kinase. / Izawa, Ichiro; Tamaki, Norihiko; Saya, Hideyuki.

In: FEBS Letters, Vol. 382, No. 1-2, 11.03.1996, p. 53-59.

Research output: Contribution to journalArticle

@article{cf1a93e860e34b69837566dd3dda14a4,
title = "Phosphorylation of neurofibromatosis type 1 gene product (neurofibromin) by cAMP-dependent protein kinase",
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.",
keywords = "cAMP-dependent protein kinase, Neurofibromatosis type 1 (NF1), Neurofibromin, Phosphorylation",
author = "Ichiro Izawa and Norihiko Tamaki and Hideyuki Saya",
year = "1996",
month = "3",
day = "11",
doi = "10.1016/0014-5793(96)00137-8",
language = "English",
volume = "382",
pages = "53--59",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1-2",

}

TY - JOUR

T1 - Phosphorylation of neurofibromatosis type 1 gene product (neurofibromin) by cAMP-dependent protein kinase

AU - Izawa, Ichiro

AU - Tamaki, Norihiko

AU - Saya, Hideyuki

PY - 1996/3/11

Y1 - 1996/3/11

N2 - 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.

AB - 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.

KW - cAMP-dependent protein kinase

KW - Neurofibromatosis type 1 (NF1)

KW - Neurofibromin

KW - Phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=0029897881&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029897881&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(96)00137-8

DO - 10.1016/0014-5793(96)00137-8

M3 - Article

VL - 382

SP - 53

EP - 59

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-2

ER -