Abstract
Signal-transducing GTP-binding proteins (G proteins) are membrane-bound coupling proteins that link the activation of cell surface receptors to changes in specific enzyme activities intracellularly, resulting in altered cellular behavior. These G proteins are heterotrimers which, upon binding of ligand-activated receptors, exchange the GDP bound to the a subunit for GTP and dissociate into the component GTP-bound α and βγ subunits. These dissociated G protein subunits then interact with and modulate the activity of specific effector systems to which they are linked. Effector systems known to be coupled by G proteins include adenylate cyclase (Gilman, 1987); cAMP and cGMP phosphodiesterase (Elks et al.. 1983; Fung et al., 1981); the Ca++, Na + and K+ ion channels (see review, Dunlap et al., 1987); phospholipase C (Cockcroft and Gomperts, 1985; Ohta et al., 1985) and phospholipase A2 (Jelsema, 1987; Fuse and Tai, 1987; Axelrod et al., 1988).
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© 1990 Plenum Press, New York
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Jelsema, C.L., Ma, A.D. (1990). The Role of GTP-Binding Proteins in the Regulation of Phospholipase A2 and C in Bovine Retinal Rod Outer Segments. 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_30
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DOI: https://doi.org/10.1007/978-1-4613-0559-0_30
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