Diffusion of the mu opioid receptor at the surface of human neuroblastoma SH-SY5Y cells is restricted to permeable domains

FEBS Lett. 2006 Oct 2;580(22):5227-31. doi: 10.1016/j.febslet.2006.08.056. Epub 2006 Sep 5.


Previous single-molecule studies have shown a long-term diffusion superimposed to a short-term confinement of the human mu opioid (hMOP) receptors at the surface of heterologous cells. However, additional ensemble average measurements are required to reach a complete understanding of the undergoing process. Here, we analyse, by fluorescence recovery after photobleaching measurements, the lateral diffusion of fully functional T7-EGFP-hMOP receptors in neuroblastoma SH-SY5Y cells naturally expressing a low level of the wild-type receptor. Experiments carried out at variable observation radii demonstrate the restriction of the receptors diffusion to sub-micrometer sized domains. Furthermore, consistently with the long-term single-molecule data, the domains are found permeable.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell Membrane Permeability* / genetics
  • Diffusion
  • Fluorescence Recovery After Photobleaching / methods
  • Humans
  • Membrane Microdomains / genetics
  • Membrane Microdomains / metabolism*
  • Microscopy, Fluorescence / methods
  • Neuroblastoma / metabolism*
  • Neuroblastoma / pathology
  • Photobleaching
  • Receptors, Opioid, mu / genetics
  • Receptors, Opioid, mu / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Signal Transduction*


  • Receptors, Opioid, mu
  • Recombinant Proteins