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Details on Person Two conventional PKC isoforms, PKC alpha and PKC betaII hav...
| Class:Id | Summation:443387 |
|---|---|
| _displayName | Two conventional PKC isoforms, PKC alpha and PKC betaII hav... |
| _timestamp | 2009-10-06 09:57:05 |
| created | [InstanceEdit:443386] Jupe, S, 2009-10-05 |
| literatureReference | [LiteratureReference:162393] Regulation of protein kinase B/Akt activity and Ser473 phosphorylation by protein kinase Calpha in endothelial cells [LiteratureReference:443419] Protein kinase C betaII regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion [LiteratureReference:443406] PDK2: the missing piece in the receptor tyrosine kinase signaling pathway puzzle |
| modified | [InstanceEdit:443417] Jupe, S, 2009-10-06 |
| text | Two conventional PKC isoforms, PKC alpha and PKC betaII have been shown to be capable of mediating Akt phosphorylation at S473. Overexpression of PKC alpha increased S473 phosphorylation. Inhibition of PKC alpha by dominant negative constructs or suppression of PKC alpha by siRNA decreases IGF-I-stimulated Akt1 phosphorylation at S473. PKC alpha directly phosphorylated S473 in vitro, in the presence of phospholipids and calcium, leading to partial activation of Akt1. PKC beta II co-immunoprecipitation with Akt1 was induced by Fc epsilon RI stimulation with IgE and antigen. PKC beta II directly phosphorylated Akt1 at Ser473 in vitro. IgE/antigen-stimulated mast cells from PKC beta deficient knockout mice had reduced Akt S473 phosphorylation but were restored by reconstitution of PKC betaII. |
| (summation) | [Reaction:443383] PKC alpha phosphorylates AKT1 at S473 [Rattus norvegicus] [Reaction:443390] PKCalpha/betaII phosphorylate AKT at S473 [Homo sapiens] |
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No pathways have been reviewed or authored by Two conventional PKC isoforms, PKC alpha and PKC betaII hav... (443387)
