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      Diversity of structure and function of GABA B receptors: a complexity of GABA B-mediated signaling

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          Abstract

          γ-aminobutyric acid type B (GABA B) receptors are broadly expressed in the nervous system and play an important role in neuronal excitability. GABA B receptors are G protein-coupled receptors that mediate slow and prolonged inhibitory action, via activation of Gαi/o-type proteins. GABA B receptors mediate their inhibitory action through activating inwardly rectifying K + channels, inactivating voltage-gated Ca 2+ channels, and inhibiting adenylate cyclase. Functional GABA B receptors are obligate heterodimers formed by the co-assembly of R1 and R2 subunits. It is well established that GABA B receptors interact not only with G proteins and effectors but also with various proteins. This review summarizes the structure, subunit isoforms, and function of GABA B receptors, and discusses the complexity of GABA B receptors, including how receptors are localized in specific subcellular compartments, the mechanism regulating cell surface expression and mobility of the receptors, and the diversity of receptor signaling through receptor crosstalk and interacting proteins.

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          Most cited references176

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          Metabotropic glutamate receptors: physiology, pharmacology, and disease.

          The metabotropic glutamate receptors (mGluRs) are family C G-protein-coupled receptors that participate in the modulation of synaptic transmission and neuronal excitability throughout the central nervous system. The mGluRs bind glutamate within a large extracellular domain and transmit signals through the receptor protein to intracellular signaling partners. A great deal of progress has been made in determining the mechanisms by which mGluRs are activated, proteins with which they interact, and orthosteric and allosteric ligands that can modulate receptor activity. The widespread expression of mGluRs makes these receptors particularly attractive drug targets, and recent studies continue to validate the therapeutic utility of mGluR ligands in neurological and psychiatric disorders such as Alzheimer's disease, Parkinson's disease, anxiety, depression, and schizophrenia.
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            14-3-3 proteins: structure, function, and regulation.

            The 14-3-3 proteins are a family of conserved regulatory molecules expressed in all eukaryotic cells. A striking feature of the 14-3-3 proteins is their ability to bind a multitude of functionally diverse signaling proteins, including kinases, phosphatases, and transmembrane receptors. This plethora of interacting proteins allows 14-3-3 to play important roles in a wide range of vital regulatory processes, such as mitogenic signal transduction, apoptotic cell death, and cell cycle control. In this review, we examine the structural basis for 14-3-3-ligand interactions, proposed functions of 14-3-3 in various signaling pathways, and emerging views of mechanisms that regulate 14-3-3 actions.
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              Scaffold proteins: hubs for controlling the flow of cellular information.

              The spatial and temporal organization of molecules within a cell is critical for coordinating the many distinct activities carried out by the cell. In an increasing number of biological signaling processes, scaffold proteins have been found to play a central role in physically assembling the relevant molecular components. Although most scaffolds use a simple tethering mechanism to increase the efficiency of interaction between individual partner molecules, these proteins can also exert complex allosteric control over their partners and are themselves the target of regulation. Scaffold proteins offer a simple, flexible strategy for regulating selectivity in pathways, shaping output behaviors, and achieving new responses from preexisting signaling components. As a result, scaffold proteins have been exploited by evolution, pathogens, and cellular engineers to reshape cellular behavior.
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                Author and article information

                Journal
                Proc Jpn Acad Ser B Phys Biol Sci
                Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci
                PJAB
                Proceedings of the Japan Academy. Series B, Physical and Biological Sciences
                The Japan Academy (Tokyo, Japan )
                0386-2208
                1349-2896
                11 December 2018
                : 94
                : 10
                : 390-411
                Affiliations
                [*1 ]Division of Oral Biochemistry, Graduate School of Medical and Dental Sciences, Niigata University, Niigata, Japan.
                Author notes
                []Correspondence should be addressed: M. Terunuma, Division of Oral Biochemistry, Graduate School of Medical and Dental Sciences, Niigata University, 2-5274, Gakkocho-dori, Chuo-ku, Niigata 951-8514, Japan (e-mail: mterunuma@ 123456dent.niigata-u.ac.jp ).

                (Communicated by Shigetada NAKANISHI, M.J.A.)

                Article
                pjab-94-390
                10.2183/pjab.94.026
                6374141
                30541966
                b0bd3743-5576-48b7-952f-433c3e195191
                © 2018 The Japan Academy

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 1 September 2018
                : 9 October 2018
                Categories
                Review

                Life sciences
                gabab receptors,g protein-coupled receptors,di-/oligomerization,trafficking,interacting proteins,posttranslational modification

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