Involvement of the C‐terminal domain in cell surface localization and G‐protein coupling of mGluR6

2020 ◽  
Author(s):  
Dilip Rai ◽  
Takumi Akagi ◽  
Atsushi Shimohata ◽  
Toshiyuki Ishii ◽  
Mie Gangi ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
Terminal Domain ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals The C‐terminal domain is required for mGluR6 cell‐surface localization

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Atsushi Shimohata ◽  
Dilip Rai ◽  
Takumi Akagi ◽  
Toshiyuki Ishii ◽  
Mie Gangi ◽  
...  
Keyword(s):  
Cell Surface ◽  
Terminal Domain ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals Using Ligand-Induced Conformational Change to Screen for Compounds Targeting G-Protein-Coupled Receptors

2007 ◽  
Vol 12 (2) ◽  
pp. 175-185 ◽  
Author(s):  
Brian F. O'Dowd ◽  
Mohammad Alijaniaram ◽  
Xiaodong Ji ◽  
Tuan Nguyen ◽  
Richard M. Eglen ◽  
...  
Keyword(s):  
Cell Surface ◽  
G Protein ◽  
High Throughput Screening ◽  
G Protein Coupled Receptors ◽  
Nuclear Localization Sequence ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
G Protein Coupled

The authors describe a novel drug strategy designed as a primary screen to discover either antagonist or agonist compounds targeting G-protein-coupled receptors (GPCRs). The incorporation of a nuclear localization sequence (NLS, a 5 amino acid substitution), in a location in helix 8 of the GPCR structure, resulted in ligand-independent receptor translocation from the cell surface to the nucleus. Blockade of the GPCR-NLS translocation from the cell surface was achieved by either antagonist or agonist treatments, each achieving their result in a sensitive concentration-dependent manner. GPCR-NLS translocation and blockade occurred regardless of the identity of the G-protein-coupling, and thus this assay is also ideally suited for identification of compounds targeting orphan GPCRs. The GPCR-NLS trafficking was visualized by fusion to fluorescent detectable proteins. Quantification of this effect was measured by determining the density of cell surface receptors, using enzyme fragment complementation in a manner suitable for high-throughput screening. Thus, the authors have developed a cellular assay for GPCRs suitable for compound screening without requiring prior identification of an agonist or knowledge of G-protein-coupling.

scholarly journals GIRK4 Confers Appropriate Processing and Cell Surface Localization to G-protein-gated Potassium Channels

1999 ◽  
Vol 274 (4) ◽  
pp. 2571-2582 ◽  
Author(s):  
Matthew E. Kennedy ◽  
Jan Nemec ◽  
Shawn Corey ◽  
Kevin Wickman ◽  
David E. Clapham
Keyword(s):  
Potassium Channels ◽  
Cell Surface ◽  
G Protein ◽  
Surface Localization ◽  
Cell Surface Localization
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