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J. Biol. Chem. 279 (3): 1794-1800

© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

Arabidopsis Phospholipase D{alpha}1 Interacts with the Heterotrimeric G-protein {alpha}-Subunit through a Motif Analogous to the DRY Motif in G-protein-coupled Receptors*

Jian Zhao, and Xuemin Wang{ddagger}

Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506

Abstract: Phospholipase D (PLD) and heterotrimeric G-protein both play important, diverse roles in cellular regulation and signal transduction. Here we have determined the physical interaction between plant PLD and the only canonical {alpha}-subunit (G{alpha}) of the G-protein in Arabidopsis thaliana and the molecular basis for the interaction. PLD{alpha}1 expressed in either Escherichia coli or Arabidopsis was co-precipitated with G{alpha}. PLD{alpha}1 contains a sequence motif analogous to the G{alpha}-interacting DRY motif normally conserved in G-protein-coupled receptors. Mutation of the central Lys residue PLDK564A of this motif abolished the PLD{alpha}1-G{alpha} binding, whereas mutation of the two flanking residues PLDE563A and PLDF565A decreased the binding. Addition of G{alpha} to PLD{alpha}1 inhibited PLD{alpha}1 activity, whereas the PLDK564A mutation that disrupted the G{alpha}-PLD{alpha}1 binding abolished the inhibition. GTP relieved the G{alpha} inhibition of PLD{alpha}1 activity and also inhibited the binding between PLD{alpha}1 and G{alpha}. Meanwhile, the PLD{alpha}1-G{alpha} interaction stimulated the intrinsic GTPase activity of G{alpha}. Therefore, these results have demonstrated the direct binding between G{alpha} and PLD{alpha}1, identified the DRY motif on PLD{alpha}1 as the site for the interaction, and indicated that the interaction modulates reciprocally the activities of PLD{alpha}1 and G{alpha}.

Received for publication August 27, 2003. Revision received October 28, 2003.

Note Added in Proof—A G{alpha}-interacting regulator of G-protein signaling (RGS) protein, designated AtRGS1, has been identified recently in Arabidopsis. AtRGS1 has a predicted structure similar to a GPCR and an RGS box with GTPase-accelerating activity (37).

* This work was supported by grants from the National Science Foundation and the United States Department of Agriculture. This is contribution No. 04-112-J from the Kansas Agricultural Experimental Station. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed. Tel.: 785-532-6422; Fax: 785-532-7278; E-mail: wangs{at}ksu.edu.

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