A Novel Family of Phosphatidylinositol 4-Kinases Conserved from Yeast to Humans

Phosphatidylinositolpolyphosphates (PIPs) are centrally involved in many biological processes, ranging from cell growth and organization of the actin cytoskeleton to endo- and exocytosis. Phosphorylation of phosphatidylinositol at the D-4 position, an essential step in the biosynthesis of PIPs, appe...

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Published inThe Journal of biological chemistry Vol. 276; no. 11; pp. 7705 - 7708
Main Authors Barylko, Barbara, Gerber, Stefan H., Binns, Derk D., Grichine, Nikolai, Khvotchev, Mikhail, Südhof, Thomas C., Albanesi, Joseph P.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 16.03.2001
American Society for Biochemistry and Molecular Biology
Subjects
1-phosphatidylinositol 4-kinase
1-Phosphatidylinositol 4-Kinase - chemistry
Amino Acid Sequence
Animals
Cattle
Conserved Sequence
COS Cells
Humans
Molecular Sequence Data
Molecular Weight
Phosphatidylinositolpolyphosphate
Phylogeny
Rats
Saccharomyces cerevisiae
Yeasts - enzymology
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Summary:Phosphatidylinositolpolyphosphates (PIPs) are centrally involved in many biological processes, ranging from cell growth and organization of the actin cytoskeleton to endo- and exocytosis. Phosphorylation of phosphatidylinositol at the D-4 position, an essential step in the biosynthesis of PIPs, appears to be catalyzed by two biochemically distinct enzymes. However, only one of these two enzymes has been molecularly characterized. We now describe a novel class of phosphatidylinositol 4-kinases that probably corresponds to the missing element in phosphatidylinositol metabolism. These kinases are highly conserved evolutionarily, but unrelated to previously characterized phosphatidylinositol kinases, and thus represent the founding members of a new family. The novel phosphatidylinositol 4-kinases, which are widely expressed in cells, only phosphorylate phosphatidylinositol, are potently inhibited by adenosine, but are insensitive to wortmannin or phenylarsine oxide. Although they lack an obvious transmembrane domain, they are strongly attached to membranes by palmitoylation. Our data suggest that independent pathways for phosphatidylinositol 4-phosphate synthesis emerged during evolution, possibly to allow tight temporal and spatial control over the production of this key signaling molecule.
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.C000861200