A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
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A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. / Zerangue, N; Schwappach, B; Jan, Y N; Jan, L Y.
In: NEURON, Vol. 22, No. 3, 03.1999, p. 537-48.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
AU - Zerangue, N
AU - Schwappach, B
AU - Jan, Y N
AU - Jan, L Y
PY - 1999/3
Y1 - 1999/3
N2 - 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.
AB - 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.
KW - ATP-Binding Cassette Transporters
KW - Adenosine Triphosphate/physiology
KW - Amino Acid Sequence
KW - Animals
KW - COS Cells
KW - Cell Membrane/metabolism
KW - Electrophysiology
KW - Endoplasmic Reticulum/physiology
KW - Flow Cytometry
KW - Fluorescent Antibody Technique, Direct
KW - Membrane Potentials
KW - Mice
KW - Molecular Sequence Data
KW - Oocytes
KW - Patch-Clamp Techniques
KW - Potassium Channels/biosynthesis
KW - Potassium Channels, Inwardly Rectifying
KW - Rats
KW - Receptors, Drug/biosynthesis
KW - Signal Transduction/physiology
KW - Sulfonylurea Receptors
KW - Xenopus
U2 - 10.1016/s0896-6273(00)80708-4
DO - 10.1016/s0896-6273(00)80708-4
M3 - SCORING: Journal article
C2 - 10197533
VL - 22
SP - 537
EP - 548
JO - NEURON
JF - NEURON
SN - 0896-6273
IS - 3
ER -