Visualization of Phosphoinositides That Bind Pleckstrin Homology Domains: Calcium- and Agonist-induced Dynamic Changes and Relationship to Myo-[3H]inositol-labeled Phosphoinositide Pools

doi:10.1083/jcb.143.2.501

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© The Rockefeller University Press, 0021-9525/1998//501 $5.00
The Journal of Cell Biology, Volume 143, Number 2, , 1998 501-510

Regular Articles

Visualization of Phosphoinositides That Bind Pleckstrin Homology Domains: Calcium- and Agonist-induced Dynamic Changes and Relationship to Myo-[³H]inositol-labeled Phosphoinositide Pools

Péter Várnai and Tamás Balla

Endocrinology and Reproduction Research Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-4510

Phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P₂) poolsthat bind pleckstrin homology (PH) domains were visualizedby cellular expression of a phospholipase C (PLC) ${delta}$ PH domain–greenfluorescent protein fusion construct and analysis of confocal images in living cells. Plasma membrane localization of thefluorescent probe required the presence of three basic residueswithin the PLC ${delta}$ PH domain known to form critical contacts withPtdIns(4,5)P₂. Activation of endogenous PLCs by ionophoresor by receptor stimulation produced rapid redistribution ofthe fluorescent signal from the membrane to cytosol, whichwas reversed after Ca²⁺ chelation. In both ionomycin- and agonist-stimulatedcells, fluorescent probe distribution closely correlated withchanges in absolute mass of PtdIns(4,5)P₂. Inhibition of PtdIns(4,5)P₂synthesis by quercetin or phenylarsine oxide prevented therelocalization of the fluorescent probe to the membranes after Ca²⁺ chelation in ionomycin-treated cells or during agoniststimulation. In contrast, the synthesis of the PtdIns(4,5)P₂imaged by the PH domain was not sensitive to concentrationsof wortmannin that had been found inhibitory of the synthesisof myo-[³H]inositol– labeled PtdIns(4,5)P₂. Identificationand dynamic imaging of phosphoinositides that interact withPH domains will further our understanding of the regulationof such proteins by inositol phospholipids.

Key Words: phosphoinositides • calcium • green fluorescent protein • pleckstrin-homology domain • phospholipase C

Abbreviations used in this paper: Ang II, angiotensin II; BAG, bovine adrenal glomerulosa; BAL, 2,3-dimercaptopropanol; BAPTA, 1,2-bis(2-aminophenoxy)ethane N,N,N',N-tetraacetic acid; GFP, green fluorescent protein; Ins(1,4,5)P₃, inositol-1,4,5-trisphosphate; PAO, phenylarsine oxide; PH, pleckstrin homology; PLC, phospholipase C; PtdIns, phosphatidylinositol; PtdIns(4)P, phosphatidylinositol 4-phosphate; PtdIns(4,5)P₂, phosphatidylinositol 4,5-bisphosphate; WT, wortmannin.

The skillful technical work of Ms. Y. Zhang is greatly appreciated.

Address all correspondence to T. Balla, National Institutesof Health, Bldg. 49, Rm. 6A35, 49 Convent Drive, Bethesda,MD 20892-4510. Tel.: (301) 496-2136. Fax: (301) 480-8010. E-mail:tambal{at}box-t.nih.gov

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