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Originally published In Press as doi:10.1074/jbc.M109672200 on May 17, 2002

J. Biol. Chem., Vol. 277, Issue 30, 27412-27422, July 26, 2002
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Inositol Lipid Binding and Membrane Localization of Isolated Pleckstrin Homology (PH) Domains
STUDIES ON THE PH DOMAINS OF PHOSPHOLIPASE C delta 1 AND p130*

Péter VárnaiDagger , Xuena Lin§, Sang Bong Lee||, Galina TuymetovaDagger , Tzvetanka BondevaDagger , Andras Spät**Dagger Dagger , Sue Goo Rhee||, György Hajnóczky§, and Tamas BallaDagger §§

From the Dagger  Endocrinology and Reproduction Research Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892, the § Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, || Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, and ** Department of Physiology and Laboratory of Cellular and Molecular Physiology, Semmelweis University Medical School, H-1444 Budapest, Hungary

The relationship between the ability of isolated pleckstrin homology (PH) domains to bind inositol lipids or soluble inositol phosphates in vitro and to localize to cellular membranes in live cells was examined by comparing the PH domains of phospholipase Cdelta 1 (PLCdelta 1) and the recently cloned PLC-like protein p130 fused to the green fluorescent protein (GFP). The prominent membrane localization of PLCdelta 1PH-GFP was paralleled with high affinity binding to inositol 1,4,5-trisphosphate (InsP3) as well as to phosphatidylinositol 4,5-bisphosphate-containing lipid vesicles or nitrocellulose membrane strips. In contrast, no membrane localization was observed with p130PH-GFP despite its InsP3 and phosphatidylinositol 4,5-bisphosphate-binding properties being comparable with those of PLCdelta 1PH-GFP. The N-terminal ligand binding domain of the type I InsP3 receptor also failed to localize to the plasma membrane despite its 5-fold higher affinity to InsP3 than the PH domains. By using a chimeric approach and cassette mutagenesis, the C-terminal alpha -helix and the short loop between the beta 6-beta 7 sheets of the PLCdelta 1PH domain, in addition to its InsP3-binding region, were identified as critical components for membrane localization in intact cells. These data indicate that binding to the inositol phosphate head group is necessary but may not be sufficient for membrane localization of the PLCdelta 1PH-GFP fusion protein, and motifs located within the C-terminal half of the PH domain provide auxiliary contacts with additional membrane components.

* This work was supported in part by Mobility Grant TeT 181/MO/01 from the United States-Hungarian Joint Fund (to P. V. and T. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by National Institutes of Health Grants DK51526 and GM59419 (to G. H.).

Dagger Dagger Supported by the Hungarian National Science Foundation Grant OTKA T-032270.

§§ To whom correspondence should be addressed: Rm. 6A35, Bldg. 49, 49 Convent Dr., National Institutes of Health, Bethesda, MD 20892-4510. Tel.: 301-496-2136; Fax: 301-480-8010; E-mail: tambal@box-t.nih.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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