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J Biol Chem, Vol. 273, Issue 46, 30183-30188, November 13, 1998

Interaction of the Xanthine Nucleotide Binding Goalpha Mutant with G Protein-coupled Receptors

Bo Yu and Melvin I. Simon

From the Division of Biology, 147-75, California Institute of Technology, Pasadena, California 91125

We constructed a double mutant version of the alpha  subunit of Go that was regulated by xanthine nucleotides instead of guanine nucleotides (Goalpha X). We investigated the interaction between Goalpha X and G protein-coupled receptors in vitro. First, we found that the activated m2 muscarinic cholinergic receptor (MAChR) could facilitate the exchange of XTPgamma S for XDP in the Goalpha Xbeta gamma heterotrimer. Second, the Goalpha Xbeta gamma complex was able to induce the high affinity ligand-binding state in the N-formyl peptide receptor (NFPR). These experiments demonstrated that Goalpha X was able to interact effectively with G protein-coupled receptors. Third, we found that the empty form of Goalpha X, lacking a bound nucleotide and beta gamma , formed a stable complex with the m2 muscarinic cholingeric receptor associated with the plasma membrane. Finally, we investigated the interaction of Goalpha X with receptor in COS-7 cells. The empty form of Goalpha X bound tightly to the receptor and was not activated because XTP was not available intracellularly. We tested the ability of Goalpha X to inhibit the activities of several different G protein-coupled receptors in transfected COS-7 cells and found that Goalpha X specifically inhibited Go-coupled receptors. Thus the modified G proteins may act as dominant-negative mutants to trap and inactivate specific subsets of receptors.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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