期刊
JOURNAL OF BIOCHEMISTRY
卷 163, 期 4, 页码 265-272出版社
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvx077
关键词
claudin; epithelial barrier; osmotic stress; post-translational modification; tight junction
资金
- JSPS KAKENHI [JP16H04786, JP16H01362, JP17H06012, JP16K14729, JP15KT0152, JP17J00211]
- AMED-PRIME [15664862]
- JST-PRESTO [JPMJPR12A4]
- JSPS Research Fellowship for Young Scientists [DC1]
- Grants-in-Aid for Scientific Research [17J00211, 16H01362, 17H06012, 15KT0152, 16H04786, 16K14729] Funding Source: KAKEN
Body and organ surfaces in multicellular organisms are covered with a sheet of epithelial cells. The tight junction (TJ) is an adhesive structure that seals the gap between epithelial cells and functions as a selective barrier to prevent the entry of antigens and pathogenic microbes from the extracellular environment. Several transmembrane proteins that constitute the TJ (claudin, occludin, tricellulin and angulin) have been identified. As over-expression of these proteins does not enlarge TJs or enhance epithelial barrier function, it remains unclear how TJ membrane proteins are regulated to modulate the amount of TJ and the strength of the epithelial barrier. In this review, we discuss the post-translational modifications of TJ membrane proteins and their physiological significance from the viewpoint of the dynamic regulation of the epithelial barrier.
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