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Milestone 11

Time to start FRETting

FRET

Nature Cell Biology volume 11, pages S14–S15 (2009)Cite this article

Förster's proposal was confirmed experimentally in 1967 by Lubert Stryer and Richard Haugland, who demonstrated that the phenomenon of resonance energy transfer could be used as a 'spectroscopic ruler' to determine the distance between two chromophores. These findings paved the way for using FRET to observe interactions and conformational dynamics in purified proteins in vitro.

But Förster's theory also led to another application: mapping protein distributions and interactions in living cells with high resolution using a fluorescence microscope. Fernandez and Berlin first showed in 1976 that the concept of FRET could be used to examine the dynamic distribution of receptor complexes on the cell surface. This was a substantial advance for the field because it facilitated the determination of receptor distribution with much higher spatial resolution than with standard fluorescence tagging. However, unlike the authors of work to come, Fernandez and Berlin did not show any microscopy images.

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References

PRIMARY REFERENCES

  1. Fernandez, S. M. & Berlin, R. D. Cell surface distribution of lectin receptors determined by resonance energy transfer. Nature 264, 411–415 (1976)

    Article  CAS  Google Scholar 

  2. Bacskai, B. J. et al. Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons. Science 260, 222–226 (1993)

    Article  CAS  Google Scholar 

  3. Gadella, T. W. J. Jr & Jovin, T. M. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 129, 1543–1558 (1995)

    Article  CAS  Google Scholar 

  4. Bastiaens, P. I. H. et al. Imaging the intracellular trafficking and state of the AB5 quarternary structure of cholera toxin. EMBO J. 15, 4246–4253 (1996)

    Article  CAS  Google Scholar 

FURTHER READING

  1. Förster, T. Energiewanderung und Fluoreszenz. Naturwissenschaften 6, 166–175 (1946)

    Article  Google Scholar 

  2. Stryer, L. & Haugland, R. P. Energy transfer: a spectroscopic ruler. Proc. Natl Acad. Sci. USA 58, 719–726 (1967)

    Article  CAS  Google Scholar 

  3. Kenworthy, A. K. & Edidin, M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer. J. Cell Biol. 142, 69–84 (1998)

    Article  CAS  Google Scholar 

  4. Varma, R. & Mayor, S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394, 798–801 (1998).

    Article  CAS  Google Scholar 

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  1. Associate Editor, Nature Methods,

    Allison Doerr

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  1. Allison Doerr
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Doerr, A. Time to start FRETting. Nat Cell Biol 11 (Suppl 1), S14–S15 (2009). https://doi.org/10.1038/ncb1947

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