By X. Wehrens, A. Marks
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In this approach, since the GST or GFP labels are covalently attached to the RyR, every receptor image contains the label within each of the four RyR subunits, unlike the situation for noncovalently linked ligand:RyR complexes in which ligand dissociation often complicates the analysis. Thus far, the amino terminus has been localized on the 3D structure of RyR3 using a GST fusion protein, and amino acids Asp-4365, Thr-1366, and Thr-1874, which lie within DR1, DR2, and DR3, respectively, have been located on the 3D structure of RyR2 using appropriate RyR2-GFP fusion proteins (Fig.
In grazing views of the gap, each cytoplasmic domain (or foot) has an approximately square shape and is closely associated with those of the neighboring channels to form extensive arrays. Feet arrays have a handedness, that is they appear different when viewed from the cytoplasmic or from the lumenal side of the SR membrane. The cytoplasmic domains of RyRs are mirror symmetric and also they do not abut at the corners within the arrays, but they overlap with each other by about a third of their sides.
Nascent proteins could then be truncated sequentially from the C-terminus and tagged with EGFP. Through investigation of the location of EGFP fluorescence in the cell using confocal microscopy, it was possible to determine whether the truncated protein was uniformly distributed in the cell or membrane bound. By examining the fate of the fluorescence after saponin permeabilization of the cell, it was possible to determine solubility – soluble proteins were leached out of the cell; membrane bound proteins were retained within a reticular network.