Coiled-Coil Tag−Probe System for Quick Labeling of Membrane Receptors in Living Cells

2008 ◽  
Vol 3 (6) ◽  
pp. 341-345 ◽  
Author(s):  
Yoshiaki Yano ◽  
Akiko Yano ◽  
Shinya Oishi ◽  
Yukihiko Sugimoto ◽  
Gozoh Tsujimoto ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Living Cells ◽  
Membrane Receptors ◽  
Probe System

scholarly journals How the biomimetic assembly of membrane receptors into multivalent domains is regulated by a small ligand

2021 ◽  
Author(s):  
Anna Grochmal ◽  
Ben Woods ◽  
Lilia Milanesi ◽  
Manuel Perez-Soto ◽  
Salvador Tomas
Keyword(s):  
Environmental Changes ◽  
Living Cells ◽  
Membrane Receptors

In living cells, communication requires the action of membrane receptors that are activated following very small environmental changes. A binary all-or-nothing behavior follows, making the organism extremely efficient at responding...

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.

Stoichiometric Analysis of Oligomerization of Membrane Proteins on Living Cells Using Coiled-Coil Labeling and Spectral Imaging

2013 ◽  
Vol 85 (6) ◽  
pp. 3454-3461 ◽  
Author(s):  
Kenichi Kawano ◽  
Yoshiaki Yano ◽  
Kaoru Omae ◽  
Sayaka Matsuzaki ◽  
Katsumi Matsuzaki
Keyword(s):  
Membrane Proteins ◽  
Coiled Coil ◽  
Spectral Imaging ◽  
Living Cells ◽  
Stoichiometric Analysis

scholarly journals Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export

2002 ◽  
Vol 156 (4) ◽  
pp. 617-630 ◽  
Author(s):  
Phyllis Frosst ◽  
Tinglu Guan ◽  
Cecilia Subauste ◽  
Klaus Hahn ◽  
Larry Gerace
Keyword(s):  
Nuclear Import ◽  
Nuclear Export ◽  
Nuclear Protein ◽  
Coiled Coil ◽  
Basic Amino Acid ◽  
Living Cells ◽  
Protein Export ◽  
Interphase Cells ◽  
Nuclear Injection ◽  
Amino Acid Signal

Tpr is a coiled-coil protein found near the nucleoplasmic side of the pore complex. Since neither the precise localization of Tpr nor its functions are well defined, we generated antibodies to three regions of Tpr to clarify these issues. Using light and EM immunolocalization, we determined that mammalian Tpr is concentrated within the nuclear basket of the pore complex in a distribution similar to Nup153 and Nup98. Antibody localization together with imaging of GFP-Tpr in living cells revealed that Tpr is in discrete foci inside the nucleus similar to several other nucleoporins but is not present in intranuclear filamentous networks (Zimowska et al., 1997) or in long filaments extending from the pore complex (Cordes et al., 1997) as proposed. Injection of anti-Tpr antibodies into mitotic cells resulted in depletion of Tpr from the nuclear envelope without loss of other pore complex basket proteins. Whereas nuclear import mediated by a basic amino acid signal was unaffected, nuclear export mediated by a leucine-rich signal was retarded significantly. Nuclear injection of anti-Tpr antibodies in interphase cells similarly yielded inhibition of protein export but not import. These results indicate that Tpr is a nucleoporin of the nuclear basket with a role in nuclear protein export.

Photocontrol of Coiled-Coil Proteins in Living Cells

2010 ◽  
Vol 49 (23) ◽  
pp. 3943-3946 ◽  
Author(s):  
Fuzhong Zhang ◽  
Katharina A. Timm ◽  
Katja M. Arndt ◽  
G. Andrew Woolley
Keyword(s):  
Coiled Coil ◽  
Living Cells

scholarly journals A Visualization Tool for Oligomerization and Internalization of Membrane Proteins in Living Cells: Coiled-Coil Labeling Method

2014 ◽  
Vol 134 (4) ◽  
pp. 501-506 ◽  
Author(s):  
Yoshiaki Yano ◽  
Kenichi Kawano ◽  
Kaoru Omae ◽  
Yuki Takeda ◽  
Sayaka Matsuzaki ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Coiled Coil ◽  
Living Cells ◽  
Visualization Tool ◽  
Labeling Method
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