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The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1

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The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1. / Renigunta, Vijay; Yuan, Hebao; Zuzarte, Marylou; Rinné, Susanne; Koch, Annett; Wischmeyer, Erhard; Schlichthörl, Günter; Gao, Yadong; Karschin, Andreas; Jacob, Ralf; Schwappach, Blanche; Daut, Jürgen; Preisig-Müller, Regina.

In: TRAFFIC, Vol. 7, No. 2, 02.2006, p. 168-81.

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

Harvard

Renigunta, V, Yuan, H, Zuzarte, M, Rinné, S, Koch, A, Wischmeyer, E, Schlichthörl, G, Gao, Y, Karschin, A, Jacob, R, Schwappach, B, Daut, J & Preisig-Müller, R 2006, 'The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1', TRAFFIC, vol. 7, no. 2, pp. 168-81. https://doi.org/10.1111/j.1600-0854.2005.00375.x

APA

Renigunta, V., Yuan, H., Zuzarte, M., Rinné, S., Koch, A., Wischmeyer, E., Schlichthörl, G., Gao, Y., Karschin, A., Jacob, R., Schwappach, B., Daut, J., & Preisig-Müller, R. (2006). The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1. TRAFFIC, 7(2), 168-81. https://doi.org/10.1111/j.1600-0854.2005.00375.x

Vancouver

Renigunta V, Yuan H, Zuzarte M, Rinné S, Koch A, Wischmeyer E et al. The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1. TRAFFIC. 2006 Feb;7(2):168-81. https://doi.org/10.1111/j.1600-0854.2005.00375.x

Bibtex

@article{1a91dab149744045a2779b6fd0d221fd,
title = "The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1",
abstract = "The interaction of the adaptor protein p11, also denoted S100A10, with the C-terminus of the two-pore-domain K+ channel TASK-1 was studied using yeast two-hybrid analysis, glutathione S-transferase pull-down, and co-immunoprecipitation. We found that p11 interacts with a 40 amino-acid region in the proximal C-terminus of the channel. In heterologous expression systems, deletion of the p11-interacting domain enhanced surface expression of TASK-1. Attachment of the p11-interacting domain to the cytosolic tail of the reporter protein CD8 caused retention/retrieval of the construct in the endoplasmic reticulum (ER). Attachment of the last 36 amino acids of p11 to CD8 also caused ER localization, which was abolished by removal or mutation of a putative retention motif (H/K)xKxxx, at the C-terminal end of p11. Imaging of EGFP-tagged TASK-1 channels in COS cells suggested that wild-type TASK-1 was largely retained in the ER. Knockdown of p11 with siRNA enhanced trafficking of TASK-1 to the surface membrane. Our results suggest that binding of p11 to TASK-1 retards the surface expression of the channel, most likely by virtue of a di-lysine retention signal at the C-terminus of p11. Thus, the cytosolic protein p11 may represent a 'retention factor' that causes localization of the channel to the ER.",
keywords = "14-3-3 Proteins/chemistry, Amino Acid Sequence, Animals, Annexin A2/chemistry, Binding Sites/genetics, CD8 Antigens/chemistry, CHO Cells, COS Cells, Cell Line, Chlorocebus aethiops, Cricetinae, Endoplasmic Reticulum/metabolism, Female, Humans, In Vitro Techniques, Models, Biological, Molecular Sequence Data, Mutagenesis, Site-Directed, Oocytes/metabolism, Potassium Channels, Tandem Pore Domain/chemistry, Protein Structure, Tertiary, RNA Interference, RNA, Small Interfering/genetics, Rats, Recombinant Fusion Proteins/chemistry, S100 Proteins/chemistry, Sequence Homology, Amino Acid, Two-Hybrid System Techniques, Xenopus",
author = "Vijay Renigunta and Hebao Yuan and Marylou Zuzarte and Susanne Rinn{\'e} and Annett Koch and Erhard Wischmeyer and G{\"u}nter Schlichth{\"o}rl and Yadong Gao and Andreas Karschin and Ralf Jacob and Blanche Schwappach and J{\"u}rgen Daut and Regina Preisig-M{\"u}ller",
year = "2006",
month = feb,
doi = "10.1111/j.1600-0854.2005.00375.x",
language = "English",
volume = "7",
pages = "168--81",
journal = "TRAFFIC",
issn = "1398-9219",
publisher = "Blackwell Munksgaard",
number = "2",

}

RIS

TY - JOUR

T1 - The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1

AU - Renigunta, Vijay

AU - Yuan, Hebao

AU - Zuzarte, Marylou

AU - Rinné, Susanne

AU - Koch, Annett

AU - Wischmeyer, Erhard

AU - Schlichthörl, Günter

AU - Gao, Yadong

AU - Karschin, Andreas

AU - Jacob, Ralf

AU - Schwappach, Blanche

AU - Daut, Jürgen

AU - Preisig-Müller, Regina

PY - 2006/2

Y1 - 2006/2

N2 - The interaction of the adaptor protein p11, also denoted S100A10, with the C-terminus of the two-pore-domain K+ channel TASK-1 was studied using yeast two-hybrid analysis, glutathione S-transferase pull-down, and co-immunoprecipitation. We found that p11 interacts with a 40 amino-acid region in the proximal C-terminus of the channel. In heterologous expression systems, deletion of the p11-interacting domain enhanced surface expression of TASK-1. Attachment of the p11-interacting domain to the cytosolic tail of the reporter protein CD8 caused retention/retrieval of the construct in the endoplasmic reticulum (ER). Attachment of the last 36 amino acids of p11 to CD8 also caused ER localization, which was abolished by removal or mutation of a putative retention motif (H/K)xKxxx, at the C-terminal end of p11. Imaging of EGFP-tagged TASK-1 channels in COS cells suggested that wild-type TASK-1 was largely retained in the ER. Knockdown of p11 with siRNA enhanced trafficking of TASK-1 to the surface membrane. Our results suggest that binding of p11 to TASK-1 retards the surface expression of the channel, most likely by virtue of a di-lysine retention signal at the C-terminus of p11. Thus, the cytosolic protein p11 may represent a 'retention factor' that causes localization of the channel to the ER.

AB - The interaction of the adaptor protein p11, also denoted S100A10, with the C-terminus of the two-pore-domain K+ channel TASK-1 was studied using yeast two-hybrid analysis, glutathione S-transferase pull-down, and co-immunoprecipitation. We found that p11 interacts with a 40 amino-acid region in the proximal C-terminus of the channel. In heterologous expression systems, deletion of the p11-interacting domain enhanced surface expression of TASK-1. Attachment of the p11-interacting domain to the cytosolic tail of the reporter protein CD8 caused retention/retrieval of the construct in the endoplasmic reticulum (ER). Attachment of the last 36 amino acids of p11 to CD8 also caused ER localization, which was abolished by removal or mutation of a putative retention motif (H/K)xKxxx, at the C-terminal end of p11. Imaging of EGFP-tagged TASK-1 channels in COS cells suggested that wild-type TASK-1 was largely retained in the ER. Knockdown of p11 with siRNA enhanced trafficking of TASK-1 to the surface membrane. Our results suggest that binding of p11 to TASK-1 retards the surface expression of the channel, most likely by virtue of a di-lysine retention signal at the C-terminus of p11. Thus, the cytosolic protein p11 may represent a 'retention factor' that causes localization of the channel to the ER.

KW - 14-3-3 Proteins/chemistry

KW - Amino Acid Sequence

KW - Animals

KW - Annexin A2/chemistry

KW - Binding Sites/genetics

KW - CD8 Antigens/chemistry

KW - CHO Cells

KW - COS Cells

KW - Cell Line

KW - Chlorocebus aethiops

KW - Cricetinae

KW - Endoplasmic Reticulum/metabolism

KW - Female

KW - Humans

KW - In Vitro Techniques

KW - Models, Biological

KW - Molecular Sequence Data

KW - Mutagenesis, Site-Directed

KW - Oocytes/metabolism

KW - Potassium Channels, Tandem Pore Domain/chemistry

KW - Protein Structure, Tertiary

KW - RNA Interference

KW - RNA, Small Interfering/genetics

KW - Rats

KW - Recombinant Fusion Proteins/chemistry

KW - S100 Proteins/chemistry

KW - Sequence Homology, Amino Acid

KW - Two-Hybrid System Techniques

KW - Xenopus

U2 - 10.1111/j.1600-0854.2005.00375.x

DO - 10.1111/j.1600-0854.2005.00375.x

M3 - SCORING: Journal article

C2 - 16420525

VL - 7

SP - 168

EP - 181

JO - TRAFFIC

JF - TRAFFIC

SN - 1398-9219

IS - 2

ER -