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J Biol Chem, Vol. 275, Issue 18, 13962-13966, May 5, 2000

ACCELERATED PUBLICATION
Type I Phosphatidylinositol 4-Phosphate 5-Kinase Directly Interacts with ADP-ribosylation Factor 1 and Is Responsible for Phosphatidylinositol 4,5-Bisphosphate Synthesis in the Golgi Compartment^*

David H. Jones, James B. Morris^§, Clive P. Morgan, Hisatake Kondo^¶, Robin F. Irvine, and Shamshad Cockcroft^**

From the Department of Physiology, University College London, London WC1E 6JJ, United Kingdom, the  Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QJ, United Kingdom, and the ^¶ Department of Anatomy, School of Medicine, Tohoku University, Sendai 980, Japan

Phosphatidylinositol (PtdIns) 4,5-bisphosphate is involved in many aspects of membrane traffic, but the regulation of its synthesis is only partially understood. Golgi membranes contain PI 4-kinase activity and a pool of phosphatidylinositol phosphate (PIP), which is further increased by ADP-ribosylation factor 1 (ARF1). COS7 cells were transfected with  and  forms of PI 4-kinase, and only membranes from COS7 cells transfected with PI 4-kinase  increased their content of PIP when incubated with ARF1. PtdIns(4,5)P₂ content in Golgi membranes was nonexistent but could be increased to a small extent upon adding either cytosol or Type I or Type II PIP kinases. However, when ARF1 was present, PtdIns(4,5)P₂ levels increased dramatically when membranes were incubated in the presence of cytosol or Type I, but not Type II, PIP kinase. To examine whether ARF1 could directly activate Type I PIP 5-kinase, we used an in vitro assay consisting of phosphatidycholine-containing liposomes, ARF1, and PIP 5-kinase. ARF1 increased Type I PIP 5-kinase activity in a guanine nucleotide-dependent manner, identifying this enzyme as a direct effector for ARF1.

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