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 journalArticlepeer-review

18 Citations (Scopus)


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 languageEnglish
Pages (from-to)216-222
Number of pages7
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - 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.


  • 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


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