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Diversity of structure and function of GABAB receptors: a complexity of GABAB-mediated signaling
by
TERUNUMA, Miho
in
di-/oligomerization
/ G protein-coupled receptors
/ GABAB receptors
/ interacting proteins
/ posttranslational modification
/ Review
/ trafficking
2018
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Diversity of structure and function of GABAB receptors: a complexity of GABAB-mediated signaling
by
TERUNUMA, Miho
in
di-/oligomerization
/ G protein-coupled receptors
/ GABAB receptors
/ interacting proteins
/ posttranslational modification
/ Review
/ trafficking
2018
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Diversity of structure and function of GABAB receptors: a complexity of GABAB-mediated signaling
Journal Article
Diversity of structure and function of GABAB receptors: a complexity of GABAB-mediated signaling
2018
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Overview
γ-aminobutyric acid type B (GABAB) receptors are broadly expressed in the nervous system and play an important role in neuronal excitability. GABAB receptors are G protein-coupled receptors that mediate slow and prolonged inhibitory action, via activation of Gαi/o-type proteins. GABAB receptors mediate their inhibitory action through activating inwardly rectifying K+ channels, inactivating voltage-gated Ca2+ channels, and inhibiting adenylate cyclase. Functional GABAB receptors are obligate heterodimers formed by the co-assembly of R1 and R2 subunits. It is well established that GABAB receptors interact not only with G proteins and effectors but also with various proteins. This review summarizes the structure, subunit isoforms, and function of GABAB receptors, and discusses the complexity of GABAB 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.
Publisher
The Japan Academy
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