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J Biol Chem, Vol. 274, Issue 30, 21425-21429, July 23, 1999

Selective Association of G Protein beta 4 with gamma 5 and gamma 12 Subunits in Bovine Tissues

Tomiko Asano, Rika Morishita, Hiroshi Ueda, and Kanefusa Kato

From the Department of Biochemistry, Institute for Developmental Research, Aichi Human Service Center, Kasugai, Aichi 480-0392, Japan

The beta  and gamma  subunits of G proteins are tightly bound under physiological conditions, and so far, seven beta  and 11 gamma  subunit isoforms have been found. The relative abilities of the beta  and gamma  subunits to associate with each other have been studied using transfected cell assays, in vitro translation and the yeast two-hybrid system, but have not been fully characterized in various tissues. In the present study, we demonstrated the selectivity of association of the beta  with gamma  isoforms in bovine tissues. Immunoprecipitation of beta gamma complexes from tissue extracts with antibodies against various gamma  subunits and subsequent analyses revealed that beta 4 associated with the gamma  subunits with the following rank order of selectivity: gamma 5 > gamma 12 > gamma 2 > gamma 3, while beta 2 bound to gamma 2, gamma 3, and gamma 12 more selectively than to gamma 5. By contrast, beta 1 associated with all gamma  subunits without significant selectivity. Analyses of purified beta gamma complexes containing various gamma  isoforms revealed beta  subunit compositions similar to those found in the immunoprecipitates. Particular combinations of beta  and gamma  subunit isoforms may contribute to maintaining efficient and specific signal transduction mediated by G proteins.

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