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Vol. 16, Issue 3, 1282-1295, March 2005
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* Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892;
Department of Physiology, Semmelweis University, Faculty of Medicine, 1085 Budapest, Hungary
Submitted July 9, 2004;
Revised November 17, 2004;
Accepted December 16, 2004
Monitoring Editor: Jennifer Lippincott-Schwartz
The PH domains of OSBP and FAPP1 fused to GFP were used to monitor PI(4)P distribution in COS-7 cells during manipulations of PI 4-kinase (PI4K) activities. Both domains were associated with the Golgi and small cytoplasmic vesicles, and a small fraction of OSBP-PH was found at the plasma membrane (PM). Inhibition of type-III PI4Ks with 10 µM wortmannin (Wm) significantly reduced but did not abolish Golgi localization of either PH domains. Downregulation of PI4KII
or PI4KIII
by siRNA reduced the localization of the PH domains to the Golgi and in the former case any remaining Golgi localization was eliminated by Wm treatment. PLC activation by Ca2+ ionophores dissociated the domains from all membranes, but after Ca2+ chelation, they rapidly reassociated with the Golgi, the intracellular vesicles and with the PM. PM association of the domains was significantly higher after the Ca2+ transient and was abolished by Wm pretreatment. PM relocalization was not affected by down-regulation of PI4KIII or -II, but was inhibited by down-regulation of PI4KIII, or by 10 µM PAO, which also inhibits PI4KIII. Our data suggest that these PH domains detect PI(4)P formation in extra-Golgi compartments under dynamic conditions and that various PI4Ks regulate PI(4)P synthesis in distinct cellular compartments.
Abbreviations used: BFA, brefeldin A; GFP, enhanced green fluorescent protein; mRFP, monomeric red fluorescent protein; OSBP, oxysterol-binding protein; PI, phosphatidylinositol; PI4K, phosphatidylinositol 4-kinase; PI(4)P, phosphatidylinositol 4-phosphate; PI(4,5)P2, phosphatidylinositol 4,5-bisphosphate; PH, pleckstrin homology; Wm, wortmannin.
Address correspondence to: Tamas Balla (tambal{at}box-t.nih.gov).
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