scholarly journals Lessons from Photoreceptors: Turning Off G-Protein Signaling in Living Cells

Physiology ◽  
2010 ◽  
Vol 25 (2) ◽  
pp. 72-84 ◽  
Author(s):  
Marie E. Burns ◽  
Edward N. Pugh
Keyword(s):  
G Protein ◽  
Living Cells ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Signaling System ◽  
Signaling Systems ◽  
Recent Advances ◽  
Retinal Rods

Phototransduction in retinal rods is one of the most extensively studied G-protein signaling systems. In recent years, our understanding of the biochemical steps that regulate the deactivation of the rod's response to light has greatly improved. Here, we summarize recent advances and highlight some of the remaining puzzles in this model signaling system.

Kinetics of M1muscarinic receptor and G protein signaling to phospholipase C in living cells

2010 ◽  
Vol 188 (3) ◽  
pp. i5-i5
Author(s):  
Björn H. Falkenburger ◽  
Jill B. Jensen ◽  
Bertil Hille
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Living Cells ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Kinetics Of

scholarly journals Distribution of Activator of G-Protein Signaling 3 within the Aggresomal Pathway: Role of Specific Residues in the Tetratricopeptide Repeat Domain and Differential Regulation by the AGS3 Binding Partners Giα and Mammalian Inscuteable

2010 ◽  
Vol 30 (6) ◽  
pp. 1528-1540 ◽  
Author(s):  
Ali Vural ◽  
Sadik Oner ◽  
Ningfei An ◽  
Violaine Simon ◽  
Dzwokai Ma ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Single Nucleotide ◽  
Signaling Systems ◽  
Binding Partners ◽  
Repeat Domain ◽  
Tetratricopeptide Repeat Domain ◽  
Tpr Domain

ABSTRACT AGS3, a receptor-independent activator of G-protein signaling, is involved in unexpected functional diversity for G-protein signaling systems. AGS3 has seven tetratricopeptide (TPR) motifs upstream of four G-protein regulatory (GPR) motifs that serve as docking sites for Giα-GDP. The positioning of AGS3 within the cell and the intramolecular dynamics between different domains of the proteins are likely key determinants of their ability to influence G-protein signaling. We report that AGS3 enters into the aggresome pathway and that distribution of the protein is regulated by the AGS3 binding partners Giα and mammalian Inscuteable (mInsc). Giα rescues AGS3 from the aggresome, whereas mInsc augments the aggresome-like distribution of AGS3. The distribution of AGS3 to the aggresome is dependent upon the TPR domain, and it is accelerated by disruption of the TPR organizational structure or introduction of a nonsynonymous single-nucleotide polymorphism. These data present AGS3, G-proteins, and mInsc as candidate proteins involved in regulating cellular stress associated with protein-processing pathologies.

scholarly journals Intersection of two key signal integrators in the cell: activator of G-protein signaling 3 and dishevelled-2

2020 ◽  
Vol 133 (17) ◽  
pp. jcs247908
Author(s):  
Ali Vural ◽  
Stephen M. Lanier
Keyword(s):  
Cell Surface ◽  
Signaling Pathways ◽  
G Protein ◽  
Functional Integration ◽  
Functional System ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Signaling Systems ◽  
A Cell ◽  
G Protein Coupled

ABSTRACTActivator of G-protein signaling 3 (AGS3, encoded by GPSM1) was discovered as a one of several receptor-independent activators of G-protein signaling, which are postulated to provide a platform for divergence between canonical and noncanonical G-protein signaling pathways. Similarly, Dishevelled (DVL) proteins serve as a point of divergence for β-catenin-dependent and -independent signaling pathways involving the family of Frizzled (FZD) ligands and cell-surface WNT receptors. We recently discovered the apparent regulated localization of dishevelled-2 (DVL2) and AGS3 to distinct cellular puncta, suggesting that the two proteins interact as part of various cell signaling systems. To address this hypothesis, we asked the following questions: (1) do AGS3 signaling pathways influence the activation of β-catenin (CTNNB1)-regulated transcription through the WNT–Frizzled–Dishevelled axis, and (2) is the AGS3 and DVL2 interaction regulated? The interaction of AGS3 and DVL2 was regulated by protein phosphorylation, subcellular distribution, and a cell-surface G-protein-coupled receptor. These data, and the commonality of functional system impacts observed for AGS3 and DVL2, suggest that the AGS3–DVL2 complex presents an unexpected path for functional integration within the cell.This article has an associated First Person interview with the first author of the paper.

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