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M100982200v1
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Papers In Press, published online ahead of print February 13, 2001
J. Biol. Chem, 10.1074/jbc.M100982200
Submitted on February 1, 2001
Revised on February 8, 2001
Accepted on February 12, 2001

Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family

Shane Minogue, J. Simon Anderson, Mark G. Waugh, Maria dos Santos, Steven Corless, Rainer Cramer, and J. Justin Hsuan

Centre for Molecular Cell Biology, University College London, London NW3 2PF

Corresponding Author: j.hsuan{at}rfc.ucl.ac.uk

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 IIa and a second human isoform, type IIß. The type IIa mRNA appears to be expressed ubiquitously in human tissues and homologues appear to be expressed in all eukaryotes.


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