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J Biol Chem, Vol. 275, Issue 11, 7466-7469, March 17, 2000

ACCELERATED PUBLICATION
The Pleckstrin Homology Domain of Phospholipase C-₂ Links the Binding of G to Activation of the Catalytic Core^*

Tieli Wang^§, Louisa Dowal, M. Raafat El-Maghrabi, Mario Rebecchi^¶, and Suzanne Scarlata

From the  Department of Physiology and Biophysics and the ^¶ Department of Anesthesiology, State University of New York at Stony Brook, Stony Brook, New York 11794-8661

Pleckstrin homology (PH) domains are membrane tethering devices found in many signal transducing proteins. These domains also couple to the subunits of GTP binding proteins (G proteins), but whether this association transmits allosteric information to the catalytic core is unclear. To address this question, we constructed protein chimeras in which the PH domain of phospholipase C-₂ (PLC-₂), which is regulated by G, replaces the PH domain of PLC-₁ which binds to, but is not regulated by, G. We found that attachment of the PH domain of PLC-₂ onto PLC-₁ not only causes the membrane-binding properties of PLC-₁ to become similar to those of PLC-₂, but also results in a G-regulated enzyme. Thus, PH domains are more than simple tethering devices and mediate regulatory signals to the host protein.

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