The yeast Ste2p G protein-coupled receptor dimerizes on the cell plasma membrane
| Autor: | Cagdas D Son, Jeffrey M. Becker, Orkun Cevheroğlu, Melinda Hauser, Gözde Kumaş |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins media_common.quotation_subject Cell Membrane Biophysics Cell Biology Biology Biochemistry Receptors G-Protein-Coupled Green fluorescent protein 03 medical and health sciences Bimolecular fluorescence complementation Transmembrane domain 030104 developmental biology Förster resonance energy transfer Mating of yeast Receptors Mating Factor Protein Multimerization Internalization Receptor G protein-coupled receptor media_common |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1859:698-711 |
| ISSN: | 0005-2736 |
| Popis: | 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. (C) 2017 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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