Surface expression of the Anoctamin-1 (ANO1) channel is suppressed by protein-protein interactions with beta-COP
- Authors
- Lee, Young-Sun; Bae, Yeonju; Park, Nammi; Yoo, Jae Cheal; Cho, Chang-Hoon; Ryoo, Kanghyun; Hwang, Eun Mi; Park, Jae-Yong
- Issue Date
- 24-6월-2016
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- ANO1; beta-COP; Surface expression; Yeast two-hybrid screening; Protein-protein interactions; U251 glioblastoma cells
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.475, no.2, pp.216 - 222
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 475
- Number
- 2
- Start Page
- 216
- End Page
- 222
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/88306
- DOI
- 10.1016/j.bbrc.2016.05.077
- ISSN
- 0006-291X
- 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 beta-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 beta-COP with ANO1 into HEK293T cells led to decreased the surface expression and the channel activity of ANO1. Accordingly, endogenous ANO1 was associated with beta-COP in U251 glioblastoma cells, and silencing of beta-COP enhanced surface expression and whole-cell currents of ANO1 in these cells. Taken together, these data suggest that beta-COP negatively regulates ANO1 surface expression. (C) 2016 Elsevier Inc. All rights reserved.
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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