Surface expression of the Anoctamin-1 (ANO1) channel is suppressed by protein-protein interactions with β-COP

Young Sun Lee; Yeonju Bae; Nammi Park; Jae Cheal Yoo; Chang Hoon Cho; Kanghyun Ryoo; Eun Mi Hwang; Jae Yong Park

doi:10.1016/j.bbrc.2016.05.077

Surface expression of the Anoctamin-1 (ANO1) channel is suppressed by protein-protein interactions with β-COP

Young Sun Lee, Yeonju Bae, Nammi Park, Jae Cheal Yoo, Chang Hoon Cho, Kanghyun Ryoo, Eun Mi Hwang, Jae Yong Park

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

Anoctamin-1 (ANO1) is a Ca²⁺-activated chloride channel (CaCC) that plays important physiological roles in normal and cancerous tissues. However, the plasma membrane trafficking mechanisms of ANO1 remain poorly characterized. In yeast two-hybrid screening experiments, we observed direct interactions of ANO1 with β-COP, which is a subunit of Coat Protein Complex I (COPI). This interaction was then confirmed using several in vitro and in vivo binding assays. Moreover, the cotransfection of β-COP with ANO1 into HEK293T cells led to decreased the surface expression and the channel activity of ANO1. Accordingly, endogenous ANO1 was associated with β-COP in U251 glioblastoma cells, and silencing of β-COP enhanced surface expression and whole-cell currents of ANO1 in these cells. Taken together, these data suggest that β-COP negatively regulates ANO1 surface expression.

Original language	English
Pages (from-to)	216-222
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	475
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2016.05.077
Publication status	Published - 2016 Jun 24

Bibliographical note

Funding Information:
This research was supported by the Bio-Synergy Research Project ( NRF-2014M3A9C4066463 ) through the National Research Foundation (NRF) of Korea .

Publisher Copyright:
© 2016 Elsevier Inc. All rights reserved.

Keywords

ANO1
Protein-protein interactions
Surface expression
U251 glioblastoma cells
Yeast two-hybrid screening
β-COP

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.bbrc.2016.05.077

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title = "Surface expression of the Anoctamin-1 (ANO1) channel is suppressed by protein-protein interactions with β-COP",

abstract = "Anoctamin-1 (ANO1) is a Ca2+-activated chloride channel (CaCC) that plays important physiological roles in normal and cancerous tissues. However, the plasma membrane trafficking mechanisms of ANO1 remain poorly characterized. In yeast two-hybrid screening experiments, we observed direct interactions of ANO1 with β-COP, which is a subunit of Coat Protein Complex I (COPI). This interaction was then confirmed using several in vitro and in vivo binding assays. Moreover, the cotransfection of β-COP with ANO1 into HEK293T cells led to decreased the surface expression and the channel activity of ANO1. Accordingly, endogenous ANO1 was associated with β-COP in U251 glioblastoma cells, and silencing of β-COP enhanced surface expression and whole-cell currents of ANO1 in these cells. Taken together, these data suggest that β-COP negatively regulates ANO1 surface expression.",

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note = "Funding Information: This research was supported by the Bio-Synergy Research Project ( NRF-2014M3A9C4066463 ) through the National Research Foundation (NRF) of Korea . Publisher Copyright: {\textcopyright} 2016 Elsevier Inc. All rights reserved.",

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doi = "10.1016/j.bbrc.2016.05.077",

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AU - Lee, Young Sun

AU - Bae, Yeonju

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AU - Yoo, Jae Cheal

AU - Cho, Chang Hoon

AU - Ryoo, Kanghyun

AU - Hwang, Eun Mi

AU - Park, Jae Yong

N1 - Funding Information: This research was supported by the Bio-Synergy Research Project ( NRF-2014M3A9C4066463 ) through the National Research Foundation (NRF) of Korea . Publisher Copyright: © 2016 Elsevier Inc. All rights reserved.

PY - 2016/6/24

Y1 - 2016/6/24

N2 - Anoctamin-1 (ANO1) is a Ca2+-activated chloride channel (CaCC) that plays important physiological roles in normal and cancerous tissues. However, the plasma membrane trafficking mechanisms of ANO1 remain poorly characterized. In yeast two-hybrid screening experiments, we observed direct interactions of ANO1 with β-COP, which is a subunit of Coat Protein Complex I (COPI). This interaction was then confirmed using several in vitro and in vivo binding assays. Moreover, the cotransfection of β-COP with ANO1 into HEK293T cells led to decreased the surface expression and the channel activity of ANO1. Accordingly, endogenous ANO1 was associated with β-COP in U251 glioblastoma cells, and silencing of β-COP enhanced surface expression and whole-cell currents of ANO1 in these cells. Taken together, these data suggest that β-COP negatively regulates ANO1 surface expression.

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Surface expression of the Anoctamin-1 (ANO1) channel is suppressed by protein-protein interactions with β-COP

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

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