Abstract
We identified a serine/threonine protein kinase that is associated with and phosphorylates phosphoinositide 3-kinase (PtdIns 3-kinase). The serine kinase phosphorylates both the 85- and 110-kDa subunits of PtdIns 3-kinase and purifies with it from rat liver and immunoprecipitates with antibodies raised to the 85-kDa subunit. Tryptic phosphopeptide maps indicate that p85 from polyomavirus middle T-transformed cells is phosphorylated in vivo at three sites phosphorylated in vitro by the associated serine kinase. The 85-kDa subunit of PtdIns 3-kinase is phosphorylated in vitro on serine at a stoichiometry of approximately 1 mol of phosphate per mol of p85. This phosphorylation results in a three- to sevenfold decrease in PtdIns 3-kinase activity. Dephosphorylation with protein phosphatase 2A reverses the inhibition. This suggests that the association of protein phosphatase 2A with middle T antigen may function to activate PtdIns 3-kinase.
Dates
Type | When |
---|---|
Created | 9 years, 10 months ago (Oct. 5, 2015, 8:33 p.m.) |
Deposited | 2 years, 8 months ago (Dec. 15, 2022, 9:04 a.m.) |
Indexed | 11 months, 3 weeks ago (Sept. 10, 2024, 8:36 a.m.) |
Issued | 32 years, 6 months ago (March 1, 1993) |
Published | 32 years, 6 months ago (March 1, 1993) |
Published Online | 32 years, 6 months ago (March 1, 1993) |
Published Print | 32 years, 6 months ago (March 1, 1993) |
@article{Carpenter_1993, title={A tightly associated serine/threonine protein kinase regulates phosphoinositide 3-kinase activity.}, volume={13}, ISSN={1098-5549}, url={http://dx.doi.org/10.1128/mcb.13.3.1657}, DOI={10.1128/mcb.13.3.1657}, number={3}, journal={Molecular and Cellular Biology}, publisher={Informa UK Limited}, author={Carpenter, C L and Auger, K R and Duckworth, B C and Hou, W M and Schaffhausen, B and Cantley, L C}, year={1993}, month=mar, pages={1657–1665} }