New insights into the model of dopamine D1 receptor and G-proteins interactions
| Autor: | Magdalena Tworzydło, Marta Dziedzicka-Wasylewska, Paweł Mystek, Agnieszka Polit |
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| Rok vydání: | 2015 |
| Předmět: |
G-protein coupling
Fluorescence-lifetime imaging microscopy Gs alpha subunit G-protein Context (language use) Biology Models Biological Cell membrane GPCR Dopamine receptor D1 GTP-Binding Proteins dopamine receptor FLIM–FRET Fluorescence Resonance Energy Transfer medicine Humans Tissue Distribution Chromans Molecular Biology G protein-coupled receptor Microscopy Confocal Receptors Dopamine D1 Fluorescence recovery after photobleaching Cell Biology Benzazepines Cell biology HEK293 Cells Förster resonance energy transfer medicine.anatomical_structure Dopamine receptor FRAP FLIM-FRET Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853:594-603 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2014.12.015 |
| Popis: | The details of the interaction between G-proteins and the GPCRs have been subjected to extensive investigation with structural and functional assays, but still many fundamental questions regarding this macromolecular assembly and its mechanism remain unanswered. In the context of current structural data we investigated interactions of dopamine D 1 receptor with cognate G-proteins (Gαs) in living cells, emphasizing the prevalence of preassembled D 1 -G-protein complexes. We also tested the effect of D 1 receptor presence on the dynamics of Gαs and Gαi 3 in the cellular plasma membrane. Using fluorescence resonance energy transfer (FRET) detected by fluorescence lifetime imaging microscopy (FLIM) or fluorescence recovery after photobleaching (FRAP) microscopy, we did not detect constitutive preassociated complex between D 1 receptor and G-protein in the absence of receptor activation. Our work suggests that D 1 receptor alters the distribution of Gαs and Gαi 3 subunits inside the membrane. We also find that non-activated D 1 receptor and Gαs or Gαi 3 are present in the cell membrane within the same membrane microdomains in the proximity of about 9–10 nm. |
| Databáze: | OpenAIRE |
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