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A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels

Standard

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, Jahrgang 22, Nr. 3, 03.1999, S. 537-48.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Zerangue, N, Schwappach, B, Jan, YN & Jan, LY 1999, 'A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels', NEURON, Jg. 22, Nr. 3, S. 537-48. https://doi.org/10.1016/s0896-6273(00)80708-4

APA

Zerangue, N., Schwappach, B., Jan, Y. N., & Jan, L. Y. (1999). A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. NEURON, 22(3), 537-48. https://doi.org/10.1016/s0896-6273(00)80708-4

Vancouver

Zerangue N, Schwappach B, Jan YN, Jan LY. A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. NEURON. 1999 Mär;22(3):537-48. https://doi.org/10.1016/s0896-6273(00)80708-4

Bibtex

@article{8b9a654254644d9fbca8ed7812adc3da,
title = "A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels",
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.",
keywords = "ATP-Binding Cassette Transporters, Adenosine Triphosphate/physiology, Amino Acid Sequence, Animals, COS Cells, Cell Membrane/metabolism, Electrophysiology, Endoplasmic Reticulum/physiology, Flow Cytometry, Fluorescent Antibody Technique, Direct, Membrane Potentials, Mice, Molecular Sequence Data, Oocytes, Patch-Clamp Techniques, Potassium Channels/biosynthesis, Potassium Channels, Inwardly Rectifying, Rats, Receptors, Drug/biosynthesis, Signal Transduction/physiology, Sulfonylurea Receptors, Xenopus",
author = "N Zerangue and B Schwappach and Jan, {Y N} and Jan, {L Y}",
year = "1999",
month = mar,
doi = "10.1016/s0896-6273(00)80708-4",
language = "English",
volume = "22",
pages = "537--48",
journal = "NEURON",
issn = "0896-6273",
publisher = "Cell Press",
number = "3",

}

RIS

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 -