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J Biol Chem, Vol. 274, Issue 17, 11573-11581, April 23, 1999

The Bombesin Receptor Subtypes Have Distinct G Protein Specificities

Xiaoying JianDagger , Eduardo SainzDagger , William A. Clark§, Robert T. Jensen, James F. BatteyDagger , and John K. Northup§

From the Dagger  Laboratory of Molecular Biology, National Institute on Deafness and Other Communication Disorders, Rockville, Maryland 20850,  Digestive Diseases Section, NIDDKD, National Institutes of Health, Bethesda, Maryland 20892, and § Laboratory of Cellular Biology, National Institute on Deafness and Other Communication Disorders, Rockville, Maryland 20850

We used an in situ reconstitution assay to examine the receptor coupling to purified G protein alpha  subunits by the bombesin receptor family, including gastrin-releasing peptide receptor (GRP-R), neuromedin B receptor (NMB-R), and bombesin receptor subtype 3 (BRS-3). Cells expressing GRP-R or NMB-R catalyzed the activation of squid retinal Galpha q and mouse Galpha q but not bovine retinal Galpha t or bovine brain Galpha i/o. The GRP-R- and NMB-R-catalyzed activations of Galpha q were dependent upon and enhanced by different beta gamma dimers in the same rank order as follows: bovine brain beta gamma  > beta 1gamma 2 >> beta 1gamma 1. Despite these qualitative similarities, GRP-R and NMB-R had distinct kinetic properties in receptor-G protein coupling. GRP-R had higher affinities for bovine brain beta gamma , beta 1gamma 1, and beta 1gamma 2 and squid retinal Galpha q. In addition, GRP-R showed higher catalytic activity on squid Galpha q. Like GRP-R and NMB-R, BRS-3 did not catalyze GTPgamma S binding to Galpha i/o or Galpha t. However, BRS-3 showed little, if any, coupling with squid Galpha q but clearly activated mouse Galpha q. GRP-R and NMB-R catalyzed GTPgamma S binding to both squid and mouse Galpha q, with GRP-R activating squid Galpha q more effectively, and NMB-R also showed slight preference for squid Galpha q. These studies reveal that the structurally similar bombesin receptor subtypes, in particular BRS-3, possess distinct coupling preferences among members of the Galpha q family.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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