The active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation.

@article{Goldblum2011TheAZ,
  title={The active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation.},
  author={Simeon E. Goldblum and Usha Rai and Amit Tripathi and Manjusha Thakar and Luigina De Leo and Nicola Di Toro and Tarcisio Not and Rithwik Ramachandran and Adam C. Puche and Morley D Hollenberg and Alessio Fasano},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2011},
  volume={25 1},
  pages={144-58}
}
Vibrio cholerae-derived zonula occludins toxin (Zot) is a multifunctional protein that reversibly disassembles intestinal tight junctions (tjs). Zot structure-function analysis has mapped this activity to aa 288-293, named AT1002. AT1002 reduced transepithelial electrical resistance across rat small intestine, ex vivo, as did Zot and its processed mature form, ΔG. AT1002 increased in vivo permeability to sugar tracers, whereas scrambled control peptides did not. Binding and barrier assays in… CONTINUE READING
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