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M109672200v1
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Papers In Press, published online ahead of print May 17, 2002
J. Biol. Chem, 10.1074/jbc.M109672200
Submitted on October 5, 2001
Revised on May 17, 2002
Accepted on May 17, 2002

Inositol lipid binding and membrane localization of isolated pleckstrin homology domains. Studies on the PH-domains of PLCdelta 1 and p130

Péter Várnai, Xuena Lin, Sang Bong Lee, Galina Tuymetova, Tzvetanka Bondeva, András Spät, Sue Goo Rhee, György Hajnóczky, and Tamas Balla

Endocrinology and Reproduction Research Branch, National Institutes of Health, Bethesda, MD 20892-4510

Corresponding Author: tambal{at}box-t.nih.gov

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 Cd1 (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 in spite of its InsP3 and PI(4,5)P2 binding properties being comparable to 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 in spite of its 5-fold higher affinity to InsP3 than the PH domains. Using a chimeric approach and casette mutagenesis, the C-terminal a-helix and the short loop between the beta 6-beta 7 sheets of the PLCdelta 1PH-domain were identified as critical components for membrane localization in intact cells. These data indicate that binding to the inositol phosphate headgroup 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 putative membrane components.


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