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Volume 271, Number 43, Issue of October 25, 1996 pp. 26622-26629
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Carboxyl-terminal Fragments of Phospholipase C-1 with Intrinsic G_q GTPase-activating Protein (GAP) Activity

(Received for publication, July 9, 1996, and in revised form, August 14, 1996)

From the Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9041

Fragments of the ~50 kDa COOH-terminal region of phospholipase C-1 (PLC-1¹), ranging in size from 14 to 38 kDa, were expressed in Escherichia coli, purified, and tested for their regulatory activities. As expected, none of the fragments had phospholipase activity. Several fragments, referred to as PLC tails, displayed GTPase-activating protein (GAP) activity for G_q, the G protein class that stimulates the PLC-s in response to receptors. G_q GAP activity is characteristic of intact PLC-s. In reconstituted phospholipid vesicles that contained purified G_q and m1 muscarinic cholinergic receptors, the most active tails increased agonist-stimulated, steady-state GTPase activity over 4-fold. Stimulation of steady-state GTPase by the tails depended on receptors for facilitation of GDP-GTP exchange, suggesting that the tails act by accelerating hydrolysis of bound GTP. In addition to intrinsic GAP activity, one tail with high GAP activity and others with low or minimal activity potentiated the GAP activity of intact PLC-1. Other tails inhibited PLC-1s GAP effect. Both intrinsic GAP activity and potentiation of the PLC-1 GAP effect were often biphasic, with maxima as low as 100 nM tail and declining activities at higher concentrations. Several tails inhibited either the phospholipase activity of PLC-1, its stimulation by G_q, or both. The tails thus define the region of PLC-1 that has G_q GAP activity and suggest a mechanism of action in which the COOH terminus of PLC-s can interact with G_q and with other PLC-1 molecules.

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