Dopamine Receptors: From Structure to Function

Dopamine Receptors: From Structure to Function Abstract Missale, Cristina, S. Russel Nash, Susan W. Robinson, Mohamed Jaber, and Marc G. Caron. Dopamine Receptors: From Structure to Function. Physiol. Rev. 78: 189–225, 1998. — The diverse physiological actions of dopamine are mediated by at least five distinct G protein-coupled receptor subtypes. Two D 1 -like receptor subtypes (D 1 and D 5 ) couple to the G protein G s and activate adenylyl cyclase. The other receptor subtypes belong to the D 2 -like subfamily (D 2 , D 3 , and D 4 ) and are prototypic of G protein-coupled receptors that inhibit adenylyl cyclase and activate K + channels. The genes for the D 1 and D 5 receptors are intronless, but pseudogenes of the D 5 exist. The D 2 and D 3 receptors vary in certain tissues and species as a result of alternative splicing, and the human D 4 receptor gene exhibits extensive polymorphic variation. In the central nervous system, dopamine receptors are widely expressed because they are involved in the control of locomotion, cognition, emotion, and affect as well as neuroendocrine secretion. In the periphery, dopamine receptors are present more prominently in kidney, vasculature, and pituitary, where they affect mainly sodium homeostasis, vascular tone, and hormone secretion. Numerous genetic linkage analysis studies have failed so far to reveal unequivocal evidence for the involvement of one of these receptors in the etiology of various central nervous system disorders. However, targeted deletion of several of these dopamine receptor genes in mice should provide valuable information about their physiological functions. Footnotes C. Missale was on sabbatical leave from the Division of Pharmacology, Department of Biomedical Sciences and Biotechnology, University of Brescia, Faculty of Medicine, Brescia, Italy. M. Jaber was a recipient of an EMBO long-term fellowship, and S. R. Nash was supported by a fellowship from the Japan Society for the Promotion of Science. Copyright © 1998 the American Physiological Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Physiological Reviews The American Physiological Society

Dopamine Receptors: From Structure to Function

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The American Physiological Society
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Copyright © 2011 the American Physiological Society
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0031-9333
eISSN
1522-1210
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Abstract

Abstract Missale, Cristina, S. Russel Nash, Susan W. Robinson, Mohamed Jaber, and Marc G. Caron. Dopamine Receptors: From Structure to Function. Physiol. Rev. 78: 189–225, 1998. — The diverse physiological actions of dopamine are mediated by at least five distinct G protein-coupled receptor subtypes. Two D 1 -like receptor subtypes (D 1 and D 5 ) couple to the G protein G s and activate adenylyl cyclase. The other receptor subtypes belong to the D 2 -like subfamily (D 2 , D 3 , and D 4 ) and are prototypic of G protein-coupled receptors that inhibit adenylyl cyclase and activate K + channels. The genes for the D 1 and D 5 receptors are intronless, but pseudogenes of the D 5 exist. The D 2 and D 3 receptors vary in certain tissues and species as a result of alternative splicing, and the human D 4 receptor gene exhibits extensive polymorphic variation. In the central nervous system, dopamine receptors are widely expressed because they are involved in the control of locomotion, cognition, emotion, and affect as well as neuroendocrine secretion. In the periphery, dopamine receptors are present more prominently in kidney, vasculature, and pituitary, where they affect mainly sodium homeostasis, vascular tone, and hormone secretion. Numerous genetic linkage analysis studies have failed so far to reveal unequivocal evidence for the involvement of one of these receptors in the etiology of various central nervous system disorders. However, targeted deletion of several of these dopamine receptor genes in mice should provide valuable information about their physiological functions. Footnotes C. Missale was on sabbatical leave from the Division of Pharmacology, Department of Biomedical Sciences and Biotechnology, University of Brescia, Faculty of Medicine, Brescia, Italy. M. Jaber was a recipient of an EMBO long-term fellowship, and S. R. Nash was supported by a fellowship from the Japan Society for the Promotion of Science. Copyright © 1998 the American Physiological Society

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Physiological ReviewsThe American Physiological Society

Published: Jan 1, 1998

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