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Syntaxin 16 binds to cystic fibrosis transmembrane conductance regulator and regulates its membrane trafficking in epithelial cells.

Authors
 Namyi Gu  ;  Bo-Hyung Kim  ;  HyouYoung Rhim  ;  Jae-Yong Chung  ;  Jung-Ryul Kim  ;  Hyun-Suk Shin  ;  Seo-Hyun Yoon  ;  Joo-Youn Cho  ;  Sang-Goo Shin  ;  In-Jin Jang  ;  Kyung-Sang Yu 
Citation
 JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.285(46) : 35519-35527, 2010 
Journal Title
 JOURNAL OF BIOLOGICAL CHEMISTRY 
ISSN
 0021-9258 
Issue Date
2010
MeSH
Animals ; Binding Sites ; Cell Line, Tumor ; Cell Membrane/metabolism* ; Cystic Fibrosis Transmembrane Conductance Regulator/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator/metabolism* ; Endosomes/metabolism ; Epithelial Cells/metabolism* ; HEK293 Cells ; Humans ; Immunoblotting ; Immunoprecipitation ; Protein Binding ; Protein Transport ; RNA Interference ; Rats ; Rats, Sprague-Dawley ; Syntaxin 16/genetics ; Syntaxin 16/metabolism* ; trans-Golgi Network/metabolism
Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) is a key membrane protein in the complex network of epithelial ion transporters regulating epithelial permeability. Syntaxins are one of the major determinants in the intracellular trafficking and membrane targeting of secretory proteins. In the present study we demonstrate the biochemical and functional association between CFTR and syntaxin 16 (STX16) that mediates vesicle transport within the early/late endosomes and trans-Golgi network. Immunoprecipitation experiments in rat colon and T84 human colonic epithelial cells indicate that STX16 associates with CFTR. Further analyses using the domain-specific pulldown assay reveal that the helix domain of STX16 directly interacts with the N-terminal region of CFTR. Immunostainings in rat colon and T84 cells show that CFTR and STX16 highly co-localize at the apical and subapical regions of epithelial cells. Interestingly, CFTR-associated chloride current was reduced by the knockdown of STX16 expression in T84 cells. Surface biotinylation and recycling assays indicate that the reduction in CFTR chloride current is due to decreased CFTR expression on the plasma membrane. These results suggest that STX16 mediates recycling of CFTR and constitutes an important component of CFTR trafficking machinery in intestinal epithelial cells.
Files in This Item:
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DOI
10.1074/jbc.M110.162438
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers
Yonsei Authors
Kim, Kyung Hwan(김경환)
Lee, Min Goo(이민구) ORCID logo https://orcid.org/0000-0001-7436-012X
Gee, Heon Yung(지헌영) ORCID logo https://orcid.org/0000-0002-8741-6177
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/102540
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