کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2199551 | 1099454 | 2006 | 9 صفحه PDF | دانلود رایگان |
The canonical potassium channel selectivity filter motif TVGYG was transplanted into ionotropic glutamate receptors (iGluRs) of the AMPA and NMDA subtype to test whether it renders the iGluRs K+ selective. The TVGYG motif modulated several ion pore properties of AMPA receptor as well as NMDA receptor mutants, e.g., the intra- and extracellular polyamine block, current/voltage relationships, open channel block by MK801 and Mg2+, and permeability for divalent cations. However, introduction of the selectivity filter failed to increase the K+ selectivity of homomeric AMPA and heteromeric NMDA receptor complexes, which may be due to absence of selectivity filter-stabilizing interaction sites in the iGluR pore domain.Our findings indicate that even if glutamate receptors appear to have the intrinsic capacity for K+ permeability, as is demonstrated by the prokaryotic, glutamate-gated, K+ selective GluR0, the isolated selectivity filter is not able to confer K+ permeability to the relatively unselective iGluR cation pore.
Journal: Molecular and Cellular Neuroscience - Volume 33, Issue 3, 6 November 2006, Pages 335–343