Phosphatidylinositol-3-OH kinase direct target of Ras
Open Access
- 18 August 1994
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 370 (6490) , 527-532
- https://doi.org/10.1038/370527a0
Abstract
Ras (p21ras) interacts directly with the catalytic subunit of phosphatidylinositol-3-OH kinase in a GTP-dependent manner through the Ras effector site. In vivo, dominant negative Ras mutant N17 inhibits growth factor induced production of 3′ hosphorylated phosphoinositides in PC12 cells, and transfection of Ras, but not Raf, into COS cells results in a large elevation in the level of these lipids. Therefore Ras can probably regulate phosphatidylinositol-3-OH kinase, providing a point of divergence in signalling pathways downstream of Ras.Keywords
This publication has 37 references indexed in Scilit:
- MAP kinase kinase kinase, MAP kinase kinase and MAP kinasePublished by Elsevier ,2004
- Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1Nature, 1993
- Mammalian Ras interacts directly with the serine/threonine kinase rafPublished by Elsevier ,1993
- FUNCTION AND REGULATION OF RASAnnual Review of Biochemistry, 1993
- Identification of the SH3 Domain of GAP as an Essential Sequence for Ras-GAP-Mediated SignalingScience, 1993
- GTPase-activating protein SH2-SH3 domains induce gene expression in a Ras-dependent fashion.Molecular and Cellular Biology, 1992
- Implication of GAP in Ras-dependent transactivation of a polyoma enhancer sequenceScience, 1992
- Plugging the GAPsCurrent Biology, 1991
- ras p21 and GAP inhibit coupling of muscarinic receptors to atrial K+ channelsCell, 1990
- A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic MutantsScience, 1987