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Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins

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Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins. / Zuzarte, Marylou; Heusser, Katja; Renigunta, Vijay; Schlichthörl, Günter; Rinné, Susanne; Wischmeyer, Erhard; Daut, Jürgen; Schwappach, Blanche; Preisig-Müller, Regina.

In: J PHYSIOL-LONDON, Vol. 587, No. Pt 5, 01.03.2009, p. 929-52.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Zuzarte, M, Heusser, K, Renigunta, V, Schlichthörl, G, Rinné, S, Wischmeyer, E, Daut, J, Schwappach, B & Preisig-Müller, R 2009, 'Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins', J PHYSIOL-LONDON, vol. 587, no. Pt 5, pp. 929-52. https://doi.org/10.1113/jphysiol.2008.164756

APA

Zuzarte, M., Heusser, K., Renigunta, V., Schlichthörl, G., Rinné, S., Wischmeyer, E., Daut, J., Schwappach, B., & Preisig-Müller, R. (2009). Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins. J PHYSIOL-LONDON, 587(Pt 5), 929-52. https://doi.org/10.1113/jphysiol.2008.164756

Vancouver

Zuzarte M, Heusser K, Renigunta V, Schlichthörl G, Rinné S, Wischmeyer E et al. Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins. J PHYSIOL-LONDON. 2009 Mar 1;587(Pt 5):929-52. https://doi.org/10.1113/jphysiol.2008.164756

Bibtex

@article{f18bf02f53d449c7a4b79c96f859794b,
title = "Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins",
abstract = "The two-pore-domain potassium channels TASK-1 (KCNK3) and TASK-3 (KCNK9) modulate the electrical activity of neurons and many other cell types. We expressed TASK-1, TASK-3 and related reporter constructs in Xenopus oocytes, mammalian cell lines and various yeast strains to study the mechanisms controlling their transport to the surface membrane and the role of 14-3-3 proteins. We measured potassium currents with the voltage-clamp technique and fused N- and C-terminal fragments of the channels to various reporter proteins to study changes in subcellular localisation and surface expression. Mutational analysis showed that binding of 14-3-3 proteins to the extreme C-terminus of TASK-1 and TASK-3 masks a tri-basic motif, KRR, which differs in several important aspects from canonical arginine-based (RxR) or lysine-based (KKxx) retention signals. Pulldown experiments with GST fusion proteins showed that the KRR motif in the C-terminus of TASK-3 channels was able to bind to COPI coatomer. Disabling the binding of 14-3-3, which exposes the KRR motif, caused localisation of the GFP-tagged channel protein mainly to the Golgi complex. TASK-1 and TASK-3 also possess a di-basic N-terminal retention signal, KR, whose function was found to be independent of the binding of 14-3-3. Suppression of channel surface expression with dominant-negative channel mutants revealed that interaction with 14-3-3 has no significant effect on the dimeric assembly of the channels. Our results give a comprehensive description of the mechanisms by which 14-3-3 proteins, together with N- and C-terminal sorting signals, control the intracellular traffic of TASK-1 and TASK-3.",
keywords = "14-3-3 Proteins/metabolism, Amino Acid Motifs/genetics, Amino Acid Sequence, Animals, Female, Humans, Intracellular Space/genetics, Molecular Sequence Data, Nerve Tissue Proteins/genetics, Oocytes/metabolism, Potassium Channels, Tandem Pore Domain/genetics, Protein Sorting Signals/genetics, Protein Transport/genetics, Xenopus laevis",
author = "Marylou Zuzarte and Katja Heusser and Vijay Renigunta and G{\"u}nter Schlichth{\"o}rl and Susanne Rinn{\'e} and Erhard Wischmeyer and J{\"u}rgen Daut and Blanche Schwappach and Regina Preisig-M{\"u}ller",
year = "2009",
month = mar,
day = "1",
doi = "10.1113/jphysiol.2008.164756",
language = "English",
volume = "587",
pages = "929--52",
journal = "J PHYSIOL-LONDON",
issn = "0022-3751",
publisher = "Wiley-Blackwell",
number = "Pt 5",

}

RIS

TY - JOUR

T1 - Intracellular traffic of the K+ channels TASK-1 and TASK-3: role of N- and C-terminal sorting signals and interaction with 14-3-3 proteins

AU - Zuzarte, Marylou

AU - Heusser, Katja

AU - Renigunta, Vijay

AU - Schlichthörl, Günter

AU - Rinné, Susanne

AU - Wischmeyer, Erhard

AU - Daut, Jürgen

AU - Schwappach, Blanche

AU - Preisig-Müller, Regina

PY - 2009/3/1

Y1 - 2009/3/1

N2 - The two-pore-domain potassium channels TASK-1 (KCNK3) and TASK-3 (KCNK9) modulate the electrical activity of neurons and many other cell types. We expressed TASK-1, TASK-3 and related reporter constructs in Xenopus oocytes, mammalian cell lines and various yeast strains to study the mechanisms controlling their transport to the surface membrane and the role of 14-3-3 proteins. We measured potassium currents with the voltage-clamp technique and fused N- and C-terminal fragments of the channels to various reporter proteins to study changes in subcellular localisation and surface expression. Mutational analysis showed that binding of 14-3-3 proteins to the extreme C-terminus of TASK-1 and TASK-3 masks a tri-basic motif, KRR, which differs in several important aspects from canonical arginine-based (RxR) or lysine-based (KKxx) retention signals. Pulldown experiments with GST fusion proteins showed that the KRR motif in the C-terminus of TASK-3 channels was able to bind to COPI coatomer. Disabling the binding of 14-3-3, which exposes the KRR motif, caused localisation of the GFP-tagged channel protein mainly to the Golgi complex. TASK-1 and TASK-3 also possess a di-basic N-terminal retention signal, KR, whose function was found to be independent of the binding of 14-3-3. Suppression of channel surface expression with dominant-negative channel mutants revealed that interaction with 14-3-3 has no significant effect on the dimeric assembly of the channels. Our results give a comprehensive description of the mechanisms by which 14-3-3 proteins, together with N- and C-terminal sorting signals, control the intracellular traffic of TASK-1 and TASK-3.

AB - The two-pore-domain potassium channels TASK-1 (KCNK3) and TASK-3 (KCNK9) modulate the electrical activity of neurons and many other cell types. We expressed TASK-1, TASK-3 and related reporter constructs in Xenopus oocytes, mammalian cell lines and various yeast strains to study the mechanisms controlling their transport to the surface membrane and the role of 14-3-3 proteins. We measured potassium currents with the voltage-clamp technique and fused N- and C-terminal fragments of the channels to various reporter proteins to study changes in subcellular localisation and surface expression. Mutational analysis showed that binding of 14-3-3 proteins to the extreme C-terminus of TASK-1 and TASK-3 masks a tri-basic motif, KRR, which differs in several important aspects from canonical arginine-based (RxR) or lysine-based (KKxx) retention signals. Pulldown experiments with GST fusion proteins showed that the KRR motif in the C-terminus of TASK-3 channels was able to bind to COPI coatomer. Disabling the binding of 14-3-3, which exposes the KRR motif, caused localisation of the GFP-tagged channel protein mainly to the Golgi complex. TASK-1 and TASK-3 also possess a di-basic N-terminal retention signal, KR, whose function was found to be independent of the binding of 14-3-3. Suppression of channel surface expression with dominant-negative channel mutants revealed that interaction with 14-3-3 has no significant effect on the dimeric assembly of the channels. Our results give a comprehensive description of the mechanisms by which 14-3-3 proteins, together with N- and C-terminal sorting signals, control the intracellular traffic of TASK-1 and TASK-3.

KW - 14-3-3 Proteins/metabolism

KW - Amino Acid Motifs/genetics

KW - Amino Acid Sequence

KW - Animals

KW - Female

KW - Humans

KW - Intracellular Space/genetics

KW - Molecular Sequence Data

KW - Nerve Tissue Proteins/genetics

KW - Oocytes/metabolism

KW - Potassium Channels, Tandem Pore Domain/genetics

KW - Protein Sorting Signals/genetics

KW - Protein Transport/genetics

KW - Xenopus laevis

U2 - 10.1113/jphysiol.2008.164756

DO - 10.1113/jphysiol.2008.164756

M3 - SCORING: Journal article

C2 - 19139046

VL - 587

SP - 929

EP - 952

JO - J PHYSIOL-LONDON

JF - J PHYSIOL-LONDON

SN - 0022-3751

IS - Pt 5

ER -