Applying label-free dynamic mass redistribution technology to frame signaling of G protein–coupled receptors noninvasively in living cells

2011 ◽  
Vol 6 (11) ◽  
pp. 1748-1760 ◽  
Author(s):  
Ralf Schröder ◽  
Johannes Schmidt ◽  
Stefanie Blättermann ◽  
Lucas Peters ◽  
Nicole Janssen ◽  
...  
Keyword(s):  
G Protein ◽  
Living Cells ◽  
G Protein Coupled Receptors ◽  
Label Free ◽  
Dynamic Mass ◽  
Mass Redistribution ◽  
G Protein Coupled ◽  
Free Dynamic

scholarly journals Imaging of persistent cAMP signaling by internalized G protein-coupled receptors

2010 ◽  
Vol 45 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Davide Calebiro ◽  
Viacheslav O Nikolaev ◽  
Martin J Lohse
Keyword(s):  
G Protein ◽  
Intracellular Signaling ◽  
Current Model ◽  
Living Cells ◽  
G Protein Coupled Receptors ◽  
Membrane Receptors ◽  
Optical Methods ◽  
Camp Signaling ◽  
Gpcr Signaling ◽  
G Protein Coupled

G protein-coupled receptors (GPCRs) are the largest family of plasma membrane receptors. They mediate the effects of several endogenous cues and serve as important pharmacological targets. Although many biochemical events involved in GPCR signaling have been characterized in great detail, little is known about their spatiotemporal dynamics in living cells. The recent advent of optical methods based on fluorescent resonance energy transfer allows, for the first time, to directly monitor GPCR signaling in living cells. Utilizing these methods, it has been recently possible to show that the receptors for two protein/peptide hormones, the TSH and the parathyroid hormone, continue signaling to cAMP after their internalization into endosomes. This type of intracellular signaling is persistent and apparently triggers specific cellular outcomes. Here, we review these recent data and explain the optical methods used for such studies. Based on these findings, we propose a revision of the current model of the GPCR–cAMP signaling pathway to accommodate receptor signaling at endosomes.

Applying label-free dynamic mass redistribution assay for studying endogenous FPR1 receptor signalling in human neutrophils

2017 ◽  
Vol 88 ◽  
pp. 72-78 ◽  
Author(s):  
Hanna B. Christensen ◽  
David E. Gloriam ◽  
Daniel Sejer Pedersen ◽  
Jack B. Cowland ◽  
Niels Borregaard ◽  
...  
Keyword(s):  
Human Neutrophils ◽  
Label Free ◽  
Dynamic Mass ◽  
Receptor Signalling ◽  
Mass Redistribution ◽  
Free Dynamic

scholarly journals Recruitment of Activated G Protein-coupled Receptors to Pre-existing Clathrin-coated Pits in Living Cells

2001 ◽  
Vol 277 (5) ◽  
pp. 3552-3559 ◽  
Author(s):  
Mark G. H. Scott ◽  
Alexandre Benmerah ◽  
Olivier Muntaner ◽  
Stefano Marullo
Keyword(s):  
G Protein ◽  
Living Cells ◽  
G Protein Coupled Receptors ◽  
Coated Pits ◽  
G Protein Coupled

Increasing the throughput of label-free cell assays to study the activation of G-protein-coupled receptors by using a serial agonist exposure protocol

2019 ◽  
Vol 11 (3) ◽  
pp. 99-108 ◽  
Author(s):  
J A Stolwijk ◽  
M Skiba ◽  
C Kade ◽  
G Bernhardt ◽  
A Buschauer ◽  
...  
Keyword(s):  
G Protein ◽  
Free Cell ◽  
G Protein Coupled Receptors ◽  
Label Free ◽  
Cell Assays ◽  
G Protein Coupled

Oligomerisation of G-protein-coupled receptors

2001 ◽  
Vol 114 (7) ◽  
pp. 1265-1271 ◽  
Author(s):  
G. Milligan
Keyword(s):  
Energy Transfer ◽  
Cell Surface ◽  
G Protein ◽  
Living Cells ◽  
G Protein Coupled Receptors ◽  
Intact Cells ◽  
Effective Delivery ◽  
Multiple Copies ◽  
Agonist Ligands ◽  
G Protein Coupled

A range of approaches have recently provided evidence that G-protein-coupled receptors can exist as oligomeric complexes. Both homo-oligomers, comprising multiple copies of the same gene product, and hetero-oligomers containing more than one receptor have been detected. In several, but not all, examples, the extent of oligomerisation is regulated by the presence of agonist ligands, and emerging evidence indicates that receptor hetero-oligomers can display distinct pharmacological characteristics. A chaperonin-like role for receptor oligomerisation in effective delivery of newly synthesised receptors to the cell surface is a developing concept, and recent studies have employed a series of energy-transfer techniques to explore the presence and regulation of receptor oligomerisation in living cells. However, the majority of studies have relied largely on co-immunoprecipitation techniques, and there is still little direct information on the fraction of receptors existing as oligomers in intact cells.

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