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The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3

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The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3. / Kilisch, Markus; Lytovchenko, Olga; Schwappach, Blanche; Renigunta, Vijay; Daut, Jürgen.

In: PFLUG ARCH EUR J PHY, Vol. 467, No. 5, 05.2015, p. 1105-20.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Kilisch, M, Lytovchenko, O, Schwappach, B, Renigunta, V & Daut, J 2015, 'The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3', PFLUG ARCH EUR J PHY, vol. 467, no. 5, pp. 1105-20. https://doi.org/10.1007/s00424-014-1672-2

APA

Kilisch, M., Lytovchenko, O., Schwappach, B., Renigunta, V., & Daut, J. (2015). The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3. PFLUG ARCH EUR J PHY, 467(5), 1105-20. https://doi.org/10.1007/s00424-014-1672-2

Vancouver

Kilisch M, Lytovchenko O, Schwappach B, Renigunta V, Daut J. The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3. PFLUG ARCH EUR J PHY. 2015 May;467(5):1105-20. https://doi.org/10.1007/s00424-014-1672-2

Bibtex

@article{3b35860605684187a1818a01985f473e,
title = "The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3",
abstract = "The intracellular transport of membrane proteins is controlled by trafficking signals: Short peptide motifs that mediate the contact with COPI, COPII or various clathrin-associated coat proteins. In addition, many membrane proteins interact with accessory proteins that are involved in the sorting of these proteins to different intracellular compartments. In the K2P channels, TASK-1 and TASK-3, the influence of protein-protein interactions on sorting decisions has been studied in some detail. Both TASK paralogues interact with the adaptor protein 14-3-3; TASK-1 interacts, in addition, with the adaptor protein p11 (S100A10) and the endosomal SNARE protein syntaxin-8. The role of these interacting proteins in controlling the intracellular traffic of the channels and the underlying molecular mechanisms are summarised in this review. In the case of 14-3-3, the interacting protein masks a retention signal in the C-terminus of the channel; in the case of p11, the interacting protein carries a retention signal that localises the channel to the endoplasmic reticulum; and in the case of syntaxin-8, the interacting protein carries an endocytosis signal that complements an endocytosis signal of the channel. These examples illustrate some of the mechanisms by which interacting proteins may determine the itinerary of a membrane protein within a cell and suggest that the intracellular traffic of membrane proteins may be adapted to the specific functions of that protein by multiple protein-protein interactions.",
keywords = "Animals, Cytoplasm/metabolism, Endocytosis/physiology, Endoplasmic Reticulum/metabolism, Humans, Membrane Proteins/metabolism, Potassium Channels, Tandem Pore Domain/metabolism, Protein Transport/physiology",
author = "Markus Kilisch and Olga Lytovchenko and Blanche Schwappach and Vijay Renigunta and J{\"u}rgen Daut",
year = "2015",
month = may,
doi = "10.1007/s00424-014-1672-2",
language = "English",
volume = "467",
pages = "1105--20",
journal = "PFLUG ARCH EUR J PHY",
issn = "0031-6768",
publisher = "Springer",
number = "5",

}

RIS

TY - JOUR

T1 - The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3

AU - Kilisch, Markus

AU - Lytovchenko, Olga

AU - Schwappach, Blanche

AU - Renigunta, Vijay

AU - Daut, Jürgen

PY - 2015/5

Y1 - 2015/5

N2 - The intracellular transport of membrane proteins is controlled by trafficking signals: Short peptide motifs that mediate the contact with COPI, COPII or various clathrin-associated coat proteins. In addition, many membrane proteins interact with accessory proteins that are involved in the sorting of these proteins to different intracellular compartments. In the K2P channels, TASK-1 and TASK-3, the influence of protein-protein interactions on sorting decisions has been studied in some detail. Both TASK paralogues interact with the adaptor protein 14-3-3; TASK-1 interacts, in addition, with the adaptor protein p11 (S100A10) and the endosomal SNARE protein syntaxin-8. The role of these interacting proteins in controlling the intracellular traffic of the channels and the underlying molecular mechanisms are summarised in this review. In the case of 14-3-3, the interacting protein masks a retention signal in the C-terminus of the channel; in the case of p11, the interacting protein carries a retention signal that localises the channel to the endoplasmic reticulum; and in the case of syntaxin-8, the interacting protein carries an endocytosis signal that complements an endocytosis signal of the channel. These examples illustrate some of the mechanisms by which interacting proteins may determine the itinerary of a membrane protein within a cell and suggest that the intracellular traffic of membrane proteins may be adapted to the specific functions of that protein by multiple protein-protein interactions.

AB - The intracellular transport of membrane proteins is controlled by trafficking signals: Short peptide motifs that mediate the contact with COPI, COPII or various clathrin-associated coat proteins. In addition, many membrane proteins interact with accessory proteins that are involved in the sorting of these proteins to different intracellular compartments. In the K2P channels, TASK-1 and TASK-3, the influence of protein-protein interactions on sorting decisions has been studied in some detail. Both TASK paralogues interact with the adaptor protein 14-3-3; TASK-1 interacts, in addition, with the adaptor protein p11 (S100A10) and the endosomal SNARE protein syntaxin-8. The role of these interacting proteins in controlling the intracellular traffic of the channels and the underlying molecular mechanisms are summarised in this review. In the case of 14-3-3, the interacting protein masks a retention signal in the C-terminus of the channel; in the case of p11, the interacting protein carries a retention signal that localises the channel to the endoplasmic reticulum; and in the case of syntaxin-8, the interacting protein carries an endocytosis signal that complements an endocytosis signal of the channel. These examples illustrate some of the mechanisms by which interacting proteins may determine the itinerary of a membrane protein within a cell and suggest that the intracellular traffic of membrane proteins may be adapted to the specific functions of that protein by multiple protein-protein interactions.

KW - Animals

KW - Cytoplasm/metabolism

KW - Endocytosis/physiology

KW - Endoplasmic Reticulum/metabolism

KW - Humans

KW - Membrane Proteins/metabolism

KW - Potassium Channels, Tandem Pore Domain/metabolism

KW - Protein Transport/physiology

U2 - 10.1007/s00424-014-1672-2

DO - 10.1007/s00424-014-1672-2

M3 - SCORING: Review article

C2 - 25559843

VL - 467

SP - 1105

EP - 1120

JO - PFLUG ARCH EUR J PHY

JF - PFLUG ARCH EUR J PHY

SN - 0031-6768

IS - 5

ER -