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J Biol Chem, Vol. 273, Issue 32, 20292-20299, August 7, 1998

A Novel Phosphatidylinositol-5-phosphate 4-Kinase (Phosphatidylinositol-phosphate Kinase II) Is Phosphorylated in the Endoplasmic Reticulum in Response to Mitogenic Signals

From the Department of Biochemistry, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108, Japan

Here, we identify a novel rat phosphatidylinositol-5-phosphate 4-kinase, phosphatidylinositol-phosphate kinase II (PIPKII). PIPKII comprises 420 amino acids with a molecular mass of 47,048 Da, showing greater homology to the type II and II isoforms (61.1 and 63.7% amino acid identities, respectively) of phosphatidylinositol-phosphate kinase than to the type I isoforms. It is predominantly expressed in kidney, with low expression in almost all other tissues. PIPKII was found to have phosphatidylinositol-5-phosphate 4-kinase activity as demonstrated in other type II kinases such as PIPKII. The PIPKII that is present endogenously in rat fibroblasts, PC12 cells, and rat whole brain lysate or that is exogenously overexpressed in COS-7 cells shows a doublet migrating pattern on SDS-polyacrylamide gel electrophoresis. Alkaline phosphatase treatment and metabolic labeling in [³²P]orthophosphate experiments revealed that PIPKII is phosphorylated in vivo, resulting in a shift in its electrophoretic mobility. Phosphorylation is induced by treatment of mitogens such as serum and epidermal growth factor. Immunostaining experiments and subcellular fractionation revealed that PIPKII localizes dominantly in the endoplasmic reticulum (ER). Phosphorylation also occurs in the ER. Thus, PIPKII may have an important role in the synthesis of phosphatidylinositol bisphosphate in the ER.

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