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Article
Identification of a Novel Protein, LYRIC, Localized to Tight Junctions of Polarized Epithelial Cells
Faculty Publications
  • Deborah E Britt, Rhode Island College
  • Dong-Fang Yang, Department of Medicine, Rhode Island Hospital
  • Dong-Qin Yang, Department of Medicine, Rhode Island Hospital
Document Type
Article
Date of Original Version
1-1-2004
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.

Citation Information
Deborah E Britt, Dong-Fang Yang and Dong-Qin Yang. "Identification of a Novel Protein, LYRIC, Localized to Tight Junctions of Polarized Epithelial Cells" (2004)
Available at: http://works.bepress.com/deborah_britt/6/