Identification of a novel protein, LYRIC, localized to tight junctions of polarized epithelial cells

Experimental Cell Research
D E BrittDouglas C Hixson

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.

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Citations

Nov 8, 2006·Proceedings of the National Academy of Sciences of the United States of America·Seok-Geun LeePaul B Fisher
Jun 21, 2014·Clinical & Experimental Metastasis·Sandra CasimiroLuis Costa
Sep 3, 2009·Clinical Cancer Research : an Official Journal of the American Association for Cancer Research·Guohong HuYibin Kang
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