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Physiological Reviews, Vol. 79, No. 4, October 1999, pp. 1373-1430
Copyright ©1999 by the American Physiological Society
Department of Molecular Pharmacology, Diabetes and Metabolic Diseases Research Center, University Medical Center, State University of New York/Stony Brook, Stony Brook, New York
Morris, Andrew J. and
Craig C. Malbon.
Physiological Regulation of G Protein-Linked
Signaling. J. Neurophysiol. 79: 1373-1430, 1999. Heterotrimeric G proteins in vertebrates
constitute a family molecular switches that transduce the activation of
a populous group of cell-surface receptors to a group of diverse
effector units. The receptors include the photopigments such as
rhodopsin and prominent families such as the adrenergic, muscarinic
acetylcholine, and chemokine receptors involved in regulating a broad
spectrum of responses in humans. Signals from receptors are sensed by
heterotrimeric G proteins and transduced to effectors such as adenylyl
cyclases, phospholipases, and various ion channels. Physiological
regulation of G protein-linked receptors allows for integration of
signals that directly or indirectly effect the signaling from
receptor
G proteineffector(s). Steroid hormones can regulate
signaling via transcriptional control of the activities of the genes
encoding members of G protein-linked pathways. Posttranscriptional
mechanisms are under physiological control, altering the stability of
preexisting mRNA and affording an additional level for regulation.
Protein phosphorylation, protein prenylation, and proteolysis
constitute major posttranslational mechanisms employed in the
physiological regulation of G protein-linked signaling. Drawing
upon mechanisms at all three levels, physiological regulation permits
integration of demands placed on G protein-linked signaling.
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