Diffusion of the mu opioid receptor at the surface of human neuroblastoma SH-SY5Y cells is restricted to permeable domains.
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.
Saulière
Aude
A
Institut de Pharmacologie et Biologie Structurale, UMR CNRS 5089, 205, route de Narbonne, 31077 TOULOUSE cedex, France.
Gaibelet
Gérald
G
Millot
Claire
C
Mazères
Serge
S
Lopez
André
A
Salomé
Laurence
L
D045744:Cell Line, Tumor; D002463:Cell Membrane Permeability / Q000235:genetics; D004058:Diffusion; D036681:Fluorescence Recovery After Photobleaching / Q000379:methods; D006801:Humans; D021962:Membrane Microdomains / Q000235:genetics / Q000378:metabolism*; D008856:Microscopy, Fluorescence / Q000379:methods; D009447:Neuroblastoma / Q000378:metabolism* / Q000473:pathology; D038761:Photobleaching; D017450:Receptors, Opioid, mu / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction
D017450:Receptors, Opioid, mu; D011994:Recombinant Proteins