NDLI: Function of GB1 and GB2 subunits in G protein coupling of GABAB receptors

Content Provider	PubMed Central
Author	Marta, Margeta-mitrovic Jan, Yuh Nung Jan, Lily Yeh
Copyright Year	2001
Abstract	Many G protein-coupled receptors (GPCRs) have recently been shown to dimerize, and it was suggested that dimerization may be a prerequisite for G protein coupling. γ-aminobutyric acid type B (GABAB) receptors (GPCRs for GABA, a major inhibitory neurotransmitter in the brain) are obligate heterodimers of homologous GB1 and GB2 subunits, neither of which is functional on its own. This feature of GABAB receptors allowed us to examine which of the eight intracellular segments of the heterodimeric receptor were important for G protein activation. Replacing any of the three intracellular loops of GB2 with their GB1 counterparts resulted in nonfunctional receptors. The deletion of the complete GB2 C terminus significantly attenuated the receptor function; however, the proximal 36 residues were sufficient for reconstitution of wild type-like receptor activity. In contrast, the GB1 C terminus could be deleted and GB1 intracellular loops replaced with their GB2 or mGluR1 equivalents without affecting the receptor function. In addition, a large portion of the GB1 i2 loop could be replaced with a random coil peptide without any functional consequences. Thus, GB2 intracellular segments are solely responsible for specific coupling of GABAB receptors to their physiologic effectors, Gi and G protein-activated K+ channels. These findings strongly support a model in which a single GPCR monomer is sufficient for all of the specific G protein contacts.
Related Links	http://dx.doi.org/10.1073/pnas.251554498
Ending Page	14654
Page Count	6
Starting Page	14649
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	98
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2001-12-04
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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