Phosphatidylinositol 3-kinase is activated by nerve growth factor and epidermal growth factor in PC12 cells.

Carter, A N; Downes, C P

doi:10.1016/s0021-9258(18)42077-7

Cited by 140 publications

(7 citation statements)

References 38 publications

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“…Two of the proteins detected in NK cells have relative molecular mass corresponding to that of the PI=3 kinase 85-and 110-kD subunits. The p85-kD regnlatory subunit of PI=3 kinase is a known substrate for receptor and nonreceptor protein tyrosine kinases (20,(34)(35)(36)(37). The absence of 85=kD proteins phosphorylated on tyrosine residues in the PI=3 kinase precipitates from both Fc~RIIIAot/3`z and Fc3`RIIIAc~/~'2 expressing T cells, and the observation that this subunit, precipitated from [3zp]_ labded, nonstimulated or stimulated NK cells, has similar levels of phosphorylation argue against the possibility that phosphorylation of the regulatory subunit of PI-3 kinase occurs upon Fc~KIII cross-linking.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidylinositol-3 kinase activation induced upon Fc gamma RIIIA-ligand interaction.

Kanakaraj

Duckworth

Azzoni

et al. 1994

The Journal of Experimental Medicine

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SummaryInduced activation of protein tyrosine kinase(s) is a central event in signal transduction mediated via the low affinity receptor for IgG (Fc3`RIIIA, CD16) in natural killer (NK) cells. Tyrosine phosphorylation may affect the function of several proteins directly, or indirectly by inducing their association with other tyrosine phosphorylated proteins. Here, we report that FcTRIII stimulation induces activation of phosphatidylinositol (PI)-3 kinase in NK cells. Phosphotyrosine immunoprecipitates from FcTRIII-stimulated NK cells contain PI-kinase activity and PI-3 kinase can be directly precipitated from them. Conversely, a series of tyrosine-phosphorylated proteins is coprecipitated with PI-3 kinase from the stimulated, but not from control cells. Analogous results obtained using Jurkat T ceUs expressing transfected Fc3'RIIIAol ligand binding chain in association with 3'2 or ('2 homodimers indicate that both complexes transduce this effect, although the FcTRIIIA-~'2 complexes do so with greater efficiency. Accumulation of phosphoinositide D3 phosphorylated products in stimulated ceUs confirms PI-3 kinase activation, indicating the participation of this enzyme in FcTRIIIA-mediated signal transduction.

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Section: Discussionmentioning

confidence: 99%

Phosphatidylinositol-3 kinase activation induced upon Fc gamma RIIIA-ligand interaction.

Kanakaraj

Duckworth

Azzoni

et al. 1994

The Journal of Experimental Medicine

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“…Other mechanisms for G protein stimulation of PI 3-kinase also may exist. In neutrophils and U 937 cells, the G␤␥ subunit-responsive PI 3-kinase does not appear to be associated with a p85 adapter, whereas a p85-associated PI 3-kinase activity from human platelets can be activated by G␤␥ subunits (83). In platelets, a 46-kDa protein that cross-reacts with an antibody to the p85 PI 3-kinase subunit and a 100-kDa wortmannin-binding protein may be responsible for G␤␥ subunit-stimulated PI 3-kinase activity (24, 83).…”

Section: Phosphoinositide 3-kinasesmentioning

confidence: 96%

Physiological Regulation of G Protein-Linked Signaling

Morris

Malbon

1999

Physiological Reviews

403

294

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Heterotrimeric G proteins in vertebrates constitute a family molecular switches that transduce the activation of a populous group of cell-surface receptors to a group of diverse effector units. The receptors include the photopigments such as rhodopsin and prominent families such as the adrenergic, muscarinic acetylcholine, and chemokine receptors involved in regulating a broad spectrum of responses in humans. Signals from receptors are sensed by heterotrimeric G proteins and transduced to effectors such as adenylyl cyclases, phospholipases, and various ion channels. Physiological regulation of G protein-linked receptors allows for integration of signals that directly or indirectly effect the signaling from receptor-->G protein-->effector(s). Steroid hormones can regulate signaling via transcriptional control of the activities of the genes encoding members of G protein-linked pathways. Posttranscriptional mechanisms are under physiological control, altering the stability of preexisting mRNA and affording an additional level for regulation. Protein phosphorylation, protein prenylation, and proteolysis constitute major posttranslational mechanisms employed in the physiological regulation of G protein-linked signaling. Drawing upon mechanisms at all three levels, physiological regulation permits integration of demands placed on G protein-linked signaling.

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“…Phospholipid extractions were based on the method described previously [53]. Briefly, cells were washed with PBSA, collected in 1 ml 2.4 M HCl and transferred to a polypropylene test tube.…”

Section: Hplc Analysis Of Inositol Phosphatesmentioning

confidence: 99%

Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways

et al. 1996

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Phosphatidylinositol 3-kinase is activated by nerve growth factor and epidermal growth factor in PC12 cells.

Cited by 140 publications

References 38 publications

Phosphatidylinositol-3 kinase activation induced upon Fc gamma RIIIA-ligand interaction.

Phosphatidylinositol-3 kinase activation induced upon Fc gamma RIIIA-ligand interaction.

Physiological Regulation of G Protein-Linked Signaling

Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways

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