From fixed to FRAP: measuring protein mobility and activity in living cells
Experiments with fluorescence recovery after photobleaching (FRAP) started 30 years ago to visualize the lateral mobility and dynamics of fluorescent proteins in living cells. Its popularity increased when non-invasive fluorescent tagging became possible with the green fluorescent protein (GFP). Man...
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| Veröffentlicht in: | Nature cell biology 2001-06, Vol.3 (6), p.E145-E147 |
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| container_title | Nature cell biology |
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| creator | Reits, Eric A.J. Neefjes, Jacques J. |
| description | Experiments with fluorescence recovery after photobleaching (FRAP) started 30 years ago to visualize the lateral mobility and dynamics of fluorescent proteins in living cells. Its popularity increased when non-invasive fluorescent tagging became possible with the green fluorescent protein (GFP). Many researchers use GFP to study the localization of fusion proteins in fixed or living cells, but the same fluorescent proteins can also be used to study protein mobility in living cells. Here we review the potential of FRAP to study protein dynamics and activity within a single living cell. These measurements can be made with most standard confocal laser-scanning microscopes equipped with photobleaching protocols. |
| doi_str_mv | 10.1038/35078615 |
| format | Article |
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| subjects | Analysis Animals Biomedical and Life Sciences Cancer Research Cell Biology Cell hybridization Cells, Cultured Developmental Biology Experiments Fluorescence Fluorescence microscopy Green Fluorescent Proteins Humans Lasers Life Sciences Localization Luminescent Proteins - metabolism Membranes Methods Microscopy, Confocal - methods Mobility Photobleaching Protein metabolism Proteins Recombinant Fusion Proteins - metabolism Stem Cells Subcellular Fractions technology-review Viscosity |
| title | From fixed to FRAP: measuring protein mobility and activity in living cells |
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