Journal Article10.1152/AJPGI.2000.279.2.G250
Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: lessons from mutant animals and proteins.
TL;DR: The study of other claudins is expected to elucidate their contributions to creating junction structure and physiology in all epithelial tissues.
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Abstract: Tight junctions form the major paracellular barrier in epithelial tissues. Barrier-sealing properties are quite variable among cell types in terms of electrical resistance, solute and water flux, and charge selectivity. A molecular explanation for this variability appears closer following identification of the transmembrane proteins occludin and members of the claudin multigene family. For example, the human phenotype of mutations in claudin-16 suggests that it creates a channel that allows magnesium to diffuse through renal tight junctions. Similarly, a mouse knockout of claudin-11 reveals its role in formation of tight junctions in myelin and between Sertoli cells in testis. The study of other claudins is expected to elucidate their contributions to creating junction structure and physiology in all epithelial tissues.
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References
The Tight Junction Protein ZO-1 Establishes a Link between the Transmembrane Protein Occludin and the Actin Cytoskeleton
TL;DR: One functional role of ZO-1 is to organize components of the tight junction and link them to the cortical actin cytoskeleton within the epithelial tight junction.
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Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins
TL;DR: Detailed analyses showed that ZO-2 andZO-3 are recruited to the claudin-based networks through PDZ1 and PDZ2 domains of Z o-1/Zo-2/Z o-3 were also recruited to claudIn-based TJs, when introduced into cultured epithelial cells.
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Paracellin-1, a Renal Tight Junction Protein Required for Paracellular Mg2+ Resorption
David B. Simon,Yin Lu,Yin Lu,Keith A. Choate,Keith A. Choate,Heino Velazquez,Essam Al-Sabban,Manuel Praga,Giorgio Casari,Alberto Bettinelli,Giacomo Colussi,Juan Rodriguez-Soriano,David A. McCredie,David V. Milford,Sami A. Sanjad,Richard P. Lifton,Richard P. Lifton +16 more
TL;DR: Insight is provided into Mg2+ homeostasis, the role of a tight junction protein in human disease is demonstrated, and an essential component of a selective paracellular conductance is identified.
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A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts.
TL;DR: Findings suggested that claudin-1 and -2 are mainly responsible for TJ strand formation, and that occludin is an accessory protein in some function of TJ strands.
The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae.
TL;DR: Seven proteins function together in a complex required for exocytosis, and not other intracellular trafficking steps, the Exocyst, which is named after the yeast Saccharomyces cerevisiae.
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