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Originally published In Press as doi:10.1074/jbc.M100982200 on February 13, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16635-16640, May 18, 2001
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Cloning of a Human Type II Phosphatidylinositol 4-Kinase Reveals a Novel Lipid Kinase Family*

Shane MinogueDagger §, J. Simon AndersonDagger , Mark G. WaughDagger §, Maria dos SantosDagger , Steven Corless, Rainer Cramer, and J. Justin HsuanDagger §||

From the Dagger  Centre for Molecular Cell Biology, Department of Medicine, Royal Free and University College Medical School, Rowland Hill Street, London NW3 2PF, United Kingdom, and the  Ludwig Institute for Cancer Research, Courtauld Building, 91 Riding House Street, London W1P 8BT, United Kingdom

Phosphoinositide lipids regulate numerous cellular processes in all eukaryotes. The versatility of this phospholipid is provided by combinations of phosphorylation on the 3', 4', and 5' positions of the inositol head group. Two distinct structural families of phosphoinositide (PI) kinases have so far been identified and named after their prototypic members, the PI 3-kinase and phosphatidylinositol (PtdIns) phosphate kinase families, both of which have been found to contain structural homologues possessing PI 4-kinase activity. Nevertheless, the prevalent PtdIns 4-kinase activity in many mammalian cell types is conferred by the widespread type II PtdIns 4-kinase, which has so far resisted molecular characterization. We have partially purified the human type II isoform from plasma membrane rafts of human A431 epidermoid carcinoma cells and obtained peptide mass and sequence data. The results allowed the cDNA containing the full open reading frame to be cloned. The predicted amino acid sequence revealed that the type II enzyme is the prototypic member of a novel, third family of PI kinases. We have named the purified protein type IIalpha and a second human isoform, type IIbeta . The type IIalpha mRNA appears to be expressed ubiquitously in human tissues, and homologues appear to be expressed in all eukaryotes.

* 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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ303098.

§ Supported by The Wellcome Trust.

|| Wellcome Trust senior fellow in basic biomedical science. To whom correspondence should be addressed. Tel: 44-20-7433-2821; Fax: 44-20-7433-2817; E-mail: j.hsuan@rfc.ucl.ac.uk.

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