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The yeast Ste2p G protein-coupled receptor dimerizes on the cell plasma membrane
Date
2017-05-01
Author
Cevheroglu, Orkun
Kumas, Gozde
Hauser, Melinda
Becker, Jeffrey M.
Son, Çağdaş Devrim
Metadata
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This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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Dimerization of G protein-coupled receptors (GPCR) may play an important role in maturation, internalization, signaling and/or pharmacology of these receptors. However, the location where dimerization occurs is still under debate. In our study, variants of Ste2p, a yeast mating pheromone GPCR, were tagged with split EGFP (enhanced green fluorescent protein) fragments inserted between transmembrane domain seven and the C-terminus or appended to the C-terminus. Bimolecular Fluorescence Complementation (BiFC) assay was used to determine where receptor dimerization occurred during protein trafficking by monitoring generation of EGFP fluorescence, which occurred upon GPCR dimerization. Our results suggest that these tagged receptors traffic to the membrane as monomers, undergo dimerization or higher ordered oligomerization predominantly on the plasma membrane, and are internalized as dimers/oligomers. This study is the first to provide direct in vivo visualization of GPCR dimerization/oligomerization, during trafficking to and from the plasma membrane.
Subject Keywords
Ste2p
,
Split EGFP
,
Bimolecular fluorescence complementation assay (BiFC)
,
GPCR traffic
,
GPCR dimerization
URI
https://hdl.handle.net/11511/41182
Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
DOI
https://doi.org/10.1016/j.bbamem.2017.01.008
Collections
Department of Biology, Article
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O. Cevheroglu, G. Kumas, M. Hauser, J. M. Becker, and Ç. D. Son, “The yeast Ste2p G protein-coupled receptor dimerizes on the cell plasma membrane,”
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
, pp. 698–711, 2017, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/41182.