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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/6902

Title: Protein tyrosine phosphorylation activates rat splenic type II phosphatidylinositol 4-kinase in vitro
Authors: FERNANDIS, AZ
SUBRAHMANYAM, G
Keywords: phosphoinositide kinases
purification
3-kinase
invitro
binding
spleen
cells
Issue Date: 1998
Publisher: ELSEVIER SCIENCE BV
Citation: FEBS LETTERS, 441(3), 432-436
Abstract: Regulation of phosphatidylinositol I-kinase (PtdIns 4-kinase) by protein tyrosine phosphorylation has been indirect and the effects of phosphorylation are debatable. Rat splenic type II PtdIns I-kinase was phosphorylated in vitro with protein tyrosine kinases from Con A stimulated splenic lymphocytes. Stoichiometric analysis showed one mole of phosphate was incorporated per mole of PtdIns 4-kinase. Tyrosine phosphorylation increased the enzyme activity by 3-fold. Kinetic analysis showed a reduction in K-m for PtdIns and an increase in V-max. Dephosphorylation with protein phosphotyrosine phosphatase abolished the activation of PtdIns 4-kinase while protein phosphatase 2A had no effect. Protein tyrosine phosphorylation and activation of PtdIns l-kinase appear to be tissue specific. (C) 1998 Federation of European Biochemical Societies.
URI: http://dx.doi.org/10.1016/S0014-5793(98)01604-4
http://dspace.library.iitb.ac.in/xmlui/handle/10054/6902
http://hdl.handle.net/10054/6902
ISSN: 0014-5793
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