Abstract
Tight junctions (TJ) are multiprotein complexes that function to regulate paracellular transport of molecules through epithelial and endothelial cell layers. Many new tight junction-associated proteins have been identified in the past few years, and their functional roles and interactions have just begun to be elucidated. In this paper, we describe a novel protein LYsine-RIch CEACAM1 co-isolated (LYRIC) that is widely expressed and highly conserved between species. LYRIC has no conserved domains that would indicate function and does not appear to be a member of a larger protein family. Data from analysis of rat and human tissue sections and cell lines show that LYRIC colocalizes with tight junction proteins ZO-1 and occludin in polarized epithelial cells, suggesting that LYRIC is part of the tight junction complex. LYRIC dissociates from ZO-1 when junctional complexes are disrupted, and as tight junctions reform, ZO-1 relocalizes before LYRIC. These results suggest that LYRIC is most likely not a structural component required for TJ formation, but rather is recruited during the maturation of the tight junction complex.
Original language | English (US) |
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Pages (from-to) | 134-148 |
Number of pages | 15 |
Journal | Experimental Cell Research |
Volume | 300 |
Issue number | 1 |
DOIs | |
State | Published - Oct 15 2004 |
Keywords
- Cell adhesion
- LYRIC
- Liver
- Prostate
- Tight junction
- ZO-1
ASJC Scopus subject areas
- Cell Biology