Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells

By Junichi Ikenouchi, M. Furuse, Kyoko Furuse, H. Sasaki, Sachiko Tsukita, S. Tsukita. Journal of Cell Biology, 2005

766 citations recorded by the source corpus.

For epithelia to function as barriers, the intercellular space must be sealed. Sealing two adjacent cells at bicellular tight junctions (bTJs) is well described with the discovery of the claudins. Yet, there are still barrier weak points at tricellular contacts, where three cells join together. In this study, we identify tricellulin, the first integral membrane protein that is concentrated at the vertically oriented TJ strands of tricellular contacts. When tricellulin expression was suppressed with RNA interference, the epithelial barrier was compromised, and tricellular contacts and bTJs were disorganized. These findings indicate the critical function of tricellulin for formation of the epithelial barrier.

Subfields: Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/c9afb96f3646ccb21d5116eb83b8008e80acf465

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In Molecular Biology

1. Takuya Suzuki
2. C. Niessen
3. A. Buckley
4. J. Turner
5. Andrea Hartsock
6. C. V. Van Itallie
7. Gabriela Constantin
8. Gerd Krause

In Neurology

1. Takuya Suzuki
2. J. Turner
3. A. Buckley
4. C. V. Van Itallie
5. Gabriela Constantin
6. James M. Anderson
7. D. Agalliu
8. C. Niessen

Citations in the corpus

• Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. (2008, background): “Tricellulin a tight junction protein localized at tricellular junctions, may provide functional redundancy that allows for intact barrier function in the occludin null mouse [90].”
• Tight junctions/adherens junctions: basic structure and function. (2007, background): “tight junctional proteins, tricellulin is enriched only at tricellular tight junctions, where it enforces the barrier function of epithelial cell sheets (Ikenouchi et al., 2005).”
• Physiology and function of the tight junction. (2009, background): “1993) and tricellulin (Ikenouchi et al. 2005) are related tetraspanning proteins of currently unknown J.”
• Functional morphology of the blood-brain barrier in health and disease (2018, background): “Finally, a class of TJ-associated proteins such as tricellulin [53] and lipolysis-stimulated lipoprotein receptor (LSR) [79] are localised at the point of connection between three cells (so-called tricellular junctions), which are weak junctional points between cells.”
• Mucosal healing in inflammatory bowel diseases: a systematic review (2012, background): “Major macromolecular components in this apical junctional complex include occludin, claudins, junctional adhesion molecules, tricellulin and E-cadherin as transmembrane proteins.(25) 26 The expression of these proteins is tightly controlled by intracellular signalling and regulatory proteins.”
• The blood–brain barrier: Structure, regulation and drug delivery (2023, background): “98,99 103 Junction adhesion molecules mediate the early attachment in the BBB developmental processes.”
• Tight junctions at the blood brain barrier: physiological architecture and disease-associated dysregulation (2012, unknown): “It is a member of the family of TJ-associated marvel proteins (TAMP) with tricellulin (marvelD2) [15] and marvelD3 [16,17].”
• Tight Junction Pore and Leak Pathways: A Dynamic Duo (2011, background): “Moreover, each of the tight junction–associated marvel proteins (TAMPs), occludin, tricellulin, and marvelD3, as well as other tight junction proteins can be incorporated into the tight junction–like strands formed by claudins (31, 70, 71).”
• Cell Biology of Tight Junction Barrier Regulation and Mucosal Disease (2018, background): “Consistent with this, two tight junction-associated, occludin-related proteins, tricellulin (marvelD2) and marvelD3, have been identified to complete the tight junction-associated MARVEL protein (TAMP) family (Ikenouchi et al. 2005; Raleigh et al. 2010).”
• Regulation of the intestinal barrier by nutrients: The role of tight junctions (2020, background): “TJ pathways can be roughly categorized into bicellular and tricellular junctions (Ikenouchi et al., 2005).”
• Regulation of intestinal epithelial permeability by tight junctions (2012, background): “Four integral transmembrane proteins, occludin [15], claudins [16], junctional adhesion molecule (JAM) [17], and tricellulin [18], have been identified, with the claudin family consisting of at least 24 members.”
• Structure and function of claudins. (2008, background): “TJ strands consist of transmembrane proteins, such as occludin [3], tricellulin [4] and different claudins [5].”