Cloning and Characterization of a Wortmannin-sensitive Human Phosphatidylinositol 4-Kinase
Copyright policy )Cloning and Characterization of a Wortmannin-sensitive Human Phosphatidylinositol 4-Kinase
Phosphatidylinositol (PtdIns) 4-kinases catalyze the synthesis of PtdIns-4-P, the immediate precursor of PtdIns-4,5-P2. Here we report the cloning of a novel, ubiquitously expressed PtdIns 4-kinase (PI4Kbeta). The 2.4-kilobase pair cDNA encodes a putative translation product of 801 amino acids which shows greatest homology to the yeast PIK1 gene. The recombinant protein exhibits lipid kinase activity when expressed in Escherichia coli, and specific antibodies recognize a 110-kDa PtdIns 4-kinase in cell lysates. The biochemical properties of PI4Kbeta are characteristic of a type III enzyme. Interestingly, both recombinant PI4Kbeta and the endogenous protein are inhibited by 150 nM wortmannin, suggesting that we have cloned the previously described PtdIns 4-kinase that is responsible for regulating the synthesis of agonist-sensitive pools of polyphosphoinositides (Nakanishi, S., Catt, J. K., and Balla, T. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 5317-5321).
- Beth Israel Deaconess Medical Center United States
DNA, Complementary, Saccharomyces cerevisiae Proteins, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Recombinant Proteins, Androstadienes, Jurkat Cells, Phosphotransferases (Alcohol Group Acceptor), Escherichia coli, Humans, Amino Acid Sequence, Cloning, Molecular, Enzyme Inhibitors, Wortmannin, 1-Phosphatidylinositol 4-Kinase, Signal Transduction
DNA, Complementary, Saccharomyces cerevisiae Proteins, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Recombinant Proteins, Androstadienes, Jurkat Cells, Phosphotransferases (Alcohol Group Acceptor), Escherichia coli, Humans, Amino Acid Sequence, Cloning, Molecular, Enzyme Inhibitors, Wortmannin, 1-Phosphatidylinositol 4-Kinase, Signal Transduction
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