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Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels

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Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels. / Heusser, Katja; Yuan, Hebao; Neagoe, Ioana; Tarasov, Andrei I; Ashcroft, Frances M; Schwappach, Blanche.

in: J CELL SCI, Jahrgang 119, Nr. Pt 20, 15.10.2006, S. 4353-63.

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

Harvard

Heusser, K, Yuan, H, Neagoe, I, Tarasov, AI, Ashcroft, FM & Schwappach, B 2006, 'Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels', J CELL SCI, Jg. 119, Nr. Pt 20, S. 4353-63. https://doi.org/10.1242/jcs.03196

APA

Heusser, K., Yuan, H., Neagoe, I., Tarasov, A. I., Ashcroft, F. M., & Schwappach, B. (2006). Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels. J CELL SCI, 119(Pt 20), 4353-63. https://doi.org/10.1242/jcs.03196

Vancouver

Heusser K, Yuan H, Neagoe I, Tarasov AI, Ashcroft FM, Schwappach B. Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels. J CELL SCI. 2006 Okt 15;119(Pt 20):4353-63. https://doi.org/10.1242/jcs.03196

Bibtex

@article{0f5bcf71723d40e09b3754c55d916b2a,
title = "Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels",
abstract = "Arginine (Arg)-based endoplasmic reticulum (ER)-localization signals are involved in the quality control of different heteromultimeric membrane protein complexes. ATP-sensitive potassium (KATP) channels are unique because each subunit in the heterooctamer contains an Arg-based ER-localization signal. We have dissected the inactivation events that override the ER-localization activity of the eight peptide-sorting motifs. Employing a 14-3-3-scavenger construct to lower the availability of 14-3-3 proteins, we found that 14-3-3 proteins promote the cell-surface expression of heterologously expressed and native KATP channels. 14-3-3 proteins were detected in physical association with KATP channels in a pancreatic beta-cell line. Our results suggest that the Arg-based signal present in Kir6.2 is sterically masked by the SUR1 subunit. By contrast, 14-3-3 proteins functionally antagonized the Arg-based signal present in SUR1. The last ten amino acids were required for efficient 14-3-3 recruitment to multimeric forms of the Kir6.2 C-terminus. Channels containing a pore-forming subunit lacking these residues reached the cell surface inefficiently but were functionally indistinguishable from channels formed by the full-length subunits. In conclusion, 14-3-3 proteins promote the cell-surface transport of correctly assembled complexes but do not regulate the activity of KATP channels at the cell surface.",
keywords = "14-3-3 Proteins/chemistry, Adenosine Triphosphate/pharmacology, Amino Acid Sequence, Animals, Arginine/metabolism, Blotting, Western, COS Cells, Cell Line, Tumor, Cell Membrane/metabolism, Chlorocebus aethiops, Dose-Response Relationship, Drug, Female, Gene Expression/genetics, Membrane Potentials/drug effects, Membrane Proteins/genetics, Models, Biological, Molecular Sequence Data, Oocytes/drug effects, Potassium Channels, Inwardly Rectifying/genetics, Protein Binding, Protein Transport/physiology, Rats, Recombinant Fusion Proteins/genetics, Signal Transduction/physiology, Xenopus",
author = "Katja Heusser and Hebao Yuan and Ioana Neagoe and Tarasov, {Andrei I} and Ashcroft, {Frances M} and Blanche Schwappach",
year = "2006",
month = oct,
day = "15",
doi = "10.1242/jcs.03196",
language = "English",
volume = "119",
pages = "4353--63",
journal = "J CELL SCI",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "Pt 20",

}

RIS

TY - JOUR

T1 - Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels

AU - Heusser, Katja

AU - Yuan, Hebao

AU - Neagoe, Ioana

AU - Tarasov, Andrei I

AU - Ashcroft, Frances M

AU - Schwappach, Blanche

PY - 2006/10/15

Y1 - 2006/10/15

N2 - Arginine (Arg)-based endoplasmic reticulum (ER)-localization signals are involved in the quality control of different heteromultimeric membrane protein complexes. ATP-sensitive potassium (KATP) channels are unique because each subunit in the heterooctamer contains an Arg-based ER-localization signal. We have dissected the inactivation events that override the ER-localization activity of the eight peptide-sorting motifs. Employing a 14-3-3-scavenger construct to lower the availability of 14-3-3 proteins, we found that 14-3-3 proteins promote the cell-surface expression of heterologously expressed and native KATP channels. 14-3-3 proteins were detected in physical association with KATP channels in a pancreatic beta-cell line. Our results suggest that the Arg-based signal present in Kir6.2 is sterically masked by the SUR1 subunit. By contrast, 14-3-3 proteins functionally antagonized the Arg-based signal present in SUR1. The last ten amino acids were required for efficient 14-3-3 recruitment to multimeric forms of the Kir6.2 C-terminus. Channels containing a pore-forming subunit lacking these residues reached the cell surface inefficiently but were functionally indistinguishable from channels formed by the full-length subunits. In conclusion, 14-3-3 proteins promote the cell-surface transport of correctly assembled complexes but do not regulate the activity of KATP channels at the cell surface.

AB - Arginine (Arg)-based endoplasmic reticulum (ER)-localization signals are involved in the quality control of different heteromultimeric membrane protein complexes. ATP-sensitive potassium (KATP) channels are unique because each subunit in the heterooctamer contains an Arg-based ER-localization signal. We have dissected the inactivation events that override the ER-localization activity of the eight peptide-sorting motifs. Employing a 14-3-3-scavenger construct to lower the availability of 14-3-3 proteins, we found that 14-3-3 proteins promote the cell-surface expression of heterologously expressed and native KATP channels. 14-3-3 proteins were detected in physical association with KATP channels in a pancreatic beta-cell line. Our results suggest that the Arg-based signal present in Kir6.2 is sterically masked by the SUR1 subunit. By contrast, 14-3-3 proteins functionally antagonized the Arg-based signal present in SUR1. The last ten amino acids were required for efficient 14-3-3 recruitment to multimeric forms of the Kir6.2 C-terminus. Channels containing a pore-forming subunit lacking these residues reached the cell surface inefficiently but were functionally indistinguishable from channels formed by the full-length subunits. In conclusion, 14-3-3 proteins promote the cell-surface transport of correctly assembled complexes but do not regulate the activity of KATP channels at the cell surface.

KW - 14-3-3 Proteins/chemistry

KW - Adenosine Triphosphate/pharmacology

KW - Amino Acid Sequence

KW - Animals

KW - Arginine/metabolism

KW - Blotting, Western

KW - COS Cells

KW - Cell Line, Tumor

KW - Cell Membrane/metabolism

KW - Chlorocebus aethiops

KW - Dose-Response Relationship, Drug

KW - Female

KW - Gene Expression/genetics

KW - Membrane Potentials/drug effects

KW - Membrane Proteins/genetics

KW - Models, Biological

KW - Molecular Sequence Data

KW - Oocytes/drug effects

KW - Potassium Channels, Inwardly Rectifying/genetics

KW - Protein Binding

KW - Protein Transport/physiology

KW - Rats

KW - Recombinant Fusion Proteins/genetics

KW - Signal Transduction/physiology

KW - Xenopus

U2 - 10.1242/jcs.03196

DO - 10.1242/jcs.03196

M3 - SCORING: Journal article

C2 - 17038548

VL - 119

SP - 4353

EP - 4363

JO - J CELL SCI

JF - J CELL SCI

SN - 0021-9533

IS - Pt 20

ER -