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Abstract
Proper ion channel function often requires specific combinations of pore-forming alpha
and regulatory beta subunits, but little is known about the mechanisms that regulate
the surface expression of different channel combinations. Our studies of ATP-sensitive
K+ channel (K(ATP)) trafficking reveal an essential quality control function for a
trafficking motif present in each of the alpha (Kir6.1/2) and beta (SUR1) subunits
of the K(ATP) complex. We show that this novel motif for endoplasmic reticulum (ER)
retention/retrieval is required at multiple stages of K(ATP) assembly to restrict
surface expression to fully assembled and correctly regulated octameric channels.
We conclude that exposure of a three amino acid motif (RKR) can explain how assembly
of an ion channel complex is coupled to intracellular trafficking.