Abstract
The guanine nucleotide binding proteins, which couple receptors for light, hormones, neurotransmitters, chemotaxis factors to a variety of intracellular effectors, are a family of heterotrimeric proteins composed of α, ß and γ subunits (reviewed by Gilman, 1987; Lochrie and Simon, 1988; Neer and Clapham, 1988). Each of these subunits consists of a super gene family with many members. The α subunits bind guanine nucleotides and all have an intrinsic GTPase activity which hydrolyzes bound GTP to GDP. This enzymatic activity is central to the function of the G proteins since they are active in the GTP-liganded form and inactive in the GDP-liganded form. Activation of the guanine nucleotide binding proteins by guanosine nucleotide triphosphate causes dissociation of the heterotrimer into ß and ßγ subunits. Although the molecule is heterotrimeric, it is functionally a heterodimer because the ß and γ subunits do not dissociate in the native state. The ß and γ peptides can only be separated under strongly denaturing conditions (Neer, unpublished).
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© 1990 Plenum Press, New York
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Neer, E.J., Chow, YK., Garen-Fazio, S., Michel, T., Schmidt, C.J., Silbert, S. (1990). The Family of G Proteins. In: Vanderhoek, J.Y. (eds) Biology of Cellular Transducing Signals. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0559-0_9
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DOI: https://doi.org/10.1007/978-1-4613-0559-0_9
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