β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality.
Green fluorescent protein (GFP) has proven useful for the study of protein interactions and dynamics for the last twenty years. A variety of new fluorescent proteins have been developed that expand the use of available excitation spectra. We have undertaken an analysis of seven of the most useful fl...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3781101?pdf=render |
| _version_ | 1828868088793137152 |
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| author | Jaclyn Bubnell Patrick Pfister Maria L Sapar Matthew E Rogers Paul Feinstein |
| author_facet | Jaclyn Bubnell Patrick Pfister Maria L Sapar Matthew E Rogers Paul Feinstein |
| author_sort | Jaclyn Bubnell |
| collection | DOAJ |
| description | Green fluorescent protein (GFP) has proven useful for the study of protein interactions and dynamics for the last twenty years. A variety of new fluorescent proteins have been developed that expand the use of available excitation spectra. We have undertaken an analysis of seven of the most useful fluorescent proteins (XFPs), Cerulean (and mCerulean3), Teal, GFP, Venus, mCherry and TagRFP657, as fusions to the archetypal G-protein coupled receptor, the β2 adrenergic receptor (β2AR). We have characterized these β2AR::XFP fusions in respect to membrane trafficking and G-protein activation. We noticed that in the mouse neural cell line, OP 6, that membrane bound β2AR::XFP fusions robustly localized in the filopodia identical to gap::XFP fusions. All β2AR::XFP fusions show responses indistinguishable from each other and the non-fused form after isoprenaline exposure. Our results provide a platform by which G-protein coupled receptors can be dissected for their functionality. |
| first_indexed | 2024-12-13T05:24:34Z |
| format | Article |
| id | doaj.art-9526795785db4514a4a08a1b46f74503 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-13T05:24:34Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-9526795785db4514a4a08a1b46f745032022-12-21T23:58:14ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0189e7494110.1371/journal.pone.0074941β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality.Jaclyn BubnellPatrick PfisterMaria L SaparMatthew E RogersPaul FeinsteinGreen fluorescent protein (GFP) has proven useful for the study of protein interactions and dynamics for the last twenty years. A variety of new fluorescent proteins have been developed that expand the use of available excitation spectra. We have undertaken an analysis of seven of the most useful fluorescent proteins (XFPs), Cerulean (and mCerulean3), Teal, GFP, Venus, mCherry and TagRFP657, as fusions to the archetypal G-protein coupled receptor, the β2 adrenergic receptor (β2AR). We have characterized these β2AR::XFP fusions in respect to membrane trafficking and G-protein activation. We noticed that in the mouse neural cell line, OP 6, that membrane bound β2AR::XFP fusions robustly localized in the filopodia identical to gap::XFP fusions. All β2AR::XFP fusions show responses indistinguishable from each other and the non-fused form after isoprenaline exposure. Our results provide a platform by which G-protein coupled receptors can be dissected for their functionality.http://europepmc.org/articles/PMC3781101?pdf=render |
| spellingShingle | Jaclyn Bubnell Patrick Pfister Maria L Sapar Matthew E Rogers Paul Feinstein β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality. PLoS ONE |
| title | β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality. |
| title_full | β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality. |
| title_fullStr | β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality. |
| title_full_unstemmed | β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality. |
| title_short | β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality. |
| title_sort | β2 adrenergic receptor fluorescent protein fusions traffic to the plasma membrane and retain functionality |
| url | http://europepmc.org/articles/PMC3781101?pdf=render |
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