The Journal of Neuroscience, March 10, 2004, ():
Subunit Composition and Alternative Splicing Regulate Membrane Delivery of Kainate Receptors
J. Neurosci. Jaskolski et al.
24: 2506
Supplemental data
supplemental data
Files in this Data Supplement:
- Supplemental data
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Figure sup 1: Deglycosylation assay performed on brain protein extracts from transgenic mice expressing GluR6a-myc (Coussen et al, 2002). Enzymatic digestion and western blotting was performed as described (see Methods). GluR6a-myc is partly sensitive to EndoH and fully deglycosylated by PNG-F, as in transfected COS-7 cells. The predicted unglycosylated molecular weight is indicated by the black arrow head.
- supplemental data
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Figure sup 2: Cotransfection of GluR5b with GluR6a, GluR7a, KA1 or KA2. To test whether GluR5 preferentially coassembles with GluR7, KA1 or KA2 rather than with GluR6, we have cotransfected COS-7 cells with tagged GluR5b in combination with untagged GluR6a, GluR7a, KA1 and KA2. Surface expressed GluR5 subunits are shown in red, intracellular staining in green. GluR6a and GluR7a, but not KA1 or KA2, strongly enhance surface expression of GluR5b. Scale bar: 10?m.
- supplemental data
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Figure sup 3: Epitope tagged GluR5 and GluR6 isoforms form functional homomeric channels. Epitope-tagged GluR5 and GluR6 isoforms were transfected in HEK 293 cells to test for their electrophysiological response to glutamate (10mM). Representative traces of currents evoked by fast application (represented by the black upper line) in whole-cell recordings for GluR5a and GluR5b, and in outside-out patches for GluR6 isoforms, scale bars, 200ms and 200pA. No current was activated for the GluR5c isoform which is not expressed at the cell surface.
