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Originally published In Press as doi:10.1074/jbc.C000861200 on January 19, 2001

J. Biol. Chem., Vol. 276, Issue 11, 7705-7708, March 16, 2001
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ACCELERATED PUBLICATION
A Novel Family of Phosphatidylinositol 4-Kinases Conserved from Yeast to Humans*

Barbara BarylkoDagger , Stefan H. Gerber§, Derk D. BinnsDagger , Nikolai Grichine||, Mikhail Khvotchev§, Thomas C. Südhof§, and Joseph P. AlbanesiDagger **

From the Department of Dagger  Pharmacology, § Center for Basic Neuroscience, Department of Molecular Genetics, and Howard Hughes Medical Institute and the || Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390

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.

* This work was supported by Grant GM55562 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Holds a postdoctoral fellowship from the Deutsche For- schungsgemeinschaft.

** To whom correspondence should be addressed: Dept. of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9041. Tel.: 214-648-3200; Fax: 214-648-2971; E-mail: jalban@mednet.swmed.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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