Key result
Substitution of N-glycosylation sites throughout the H5 segment and its flanking regions indicated that H5 is mainly extracellular, with little or no intramembranous component.
Population
In vitro model studying the inwardly rectifying K+ channel (IRK) ROMK1
Comparison
Substitution of novel N-glycosylation sites and… vs Before tunicamycin treatment / expected topology…
Design
Preclinical
Authors
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Refines ROMK1 topology models in vitro; leaves open functional and clinical relevance for Kir channels.
Demonstrates that the putative pore-forming segment H5 of the ROMK1 channel is primarily extracellular, refining the topological model of inwardly rectifying K+ channels.
Schwalbe et al. (1996) studied this question. N-glycosylation site substitution and tunicamycin was evaluated on Topology of the IRK ROMK1 channel (N-glycosylation measured by gel shift assays and membrane currents). Substitution of N-glycosylation sites throughout the H5 segment and its flanking regions indicated that H5 is mainly extracellular, with little or no intramembranous component.
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