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XB-ART-13222
Neuron 1999 Mar 01;223:537-48. doi: 10.1016/s0896-6273(00)80708-4.
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A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels.

Zerangue N , Schwappach B , Jan YN , Jan LY .


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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.

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Species referenced: Xenopus
Genes referenced: kcnj11