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Receptor to Effector Signaling Through G-Proteins: βγ Dimers Join α Subunits in the World of Higher Eukaryotes

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Book cover GTPases in Biology II

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 108 / 2))

Abstract

Heterotrimeric signal transducing G-proteins are a complex and diverse set of highly homologous proteins involved in coupling of a large number of receptors to a variety of effectors (for details of molecular diversity in G-protein subunits and functional correlates see Chap. 11, this volume). It is now clear that in the animal kingdom α subunits of G-proteins are carriers of the signal generated by G-protein-coupled receptors. Affected systems are at least six adenylyl cyclases (ACs), at least three of the type C, phosphatidylinositol (PIP) specific phospholipases (PLCs), two and possibly three types of K+ channels, and voltage-gated Ca2+ channels of the L and N types. Regulation by G-protein α subunits may be of the positive (stimulatory) or negative (inhibitory) type. In in vitro reconstitution assays only subnanomolar concentrations of the various α subunits are needed to measure the desired regulatory activity. But what about βγ dimers, the second product of the activation reaction catalyzed by receptors?

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  1. L. Birnbaumer
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  1. Baylor College of Medicine, Department of Medicine Cell Biology and Experimental Therapeutics, Houston VA Medical Center, Room 3C-385, 2002 Holcombe Boulevard, Houston, TX, 77030, USA

    Burton F. Dickey M.D.

  2. Department of Cell Biology, Molecular Physiology and Biophysics, Medicine and Neurosciences, Baylor College of Medicine, One Baylor Plaza, Houston, TX, 77030, USA

    Lutz Birnbaumer Ph.D.

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© 1993 Springer-Verlag Berlin Heidelberg

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Birnbaumer, L. (1993). Receptor to Effector Signaling Through G-Proteins: βγ Dimers Join α Subunits in the World of Higher Eukaryotes. In: Dickey, B.F., Birnbaumer, L. (eds) GTPases in Biology II. Handbook of Experimental Pharmacology, vol 108 / 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78345-6_11

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