a membrane fusion protein αsnap is a novel regulator of epithelial apical junctions膜融合蛋白αsnap是一种新型调节器的上皮细胞顶端连接.pdfVIP

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a membrane fusion protein αsnap is a novel regulator of epithelial apical junctions膜融合蛋白αsnap是一种新型调节器的上皮细胞顶端连接.pdf

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a membrane fusion protein αsnap is a novel regulator of epithelial apical junctions膜融合蛋白αsnap是一种新型调节器的上皮细胞顶端连接

A Membrane Fusion Protein aSNAP Is a Novel Regulator of Epithelial Apical Junctions 1 1 1 2 1 Nayden G. Naydenov , Bryan Brown , Gianni Harris , Michael R. Dohn , Victor M. Morales , 1 2 1 Somesh Baranwal , Albert B. Reynolds , Andrei I. Ivanov * 1 Department of Medicine, University of Rochester, Rochester, New York, United States of America, 2 Department of Cancer Biology, Vanderbilt University, Nashville, Tennessee, United States of America Abstract Tight junctions (TJs) and adherens junctions (AJs) are key determinants of the structure and permeability of epithelial barriers. Although exocytic delivery to the cell surface is crucial for junctional assembly, little is known about the mechanisms controlling TJ and AJ exocytosis. This study was aimed at investigating whether a key mediator of exocytosis, soluble N-ethylmaleimide sensitive factor (NSF) attachment protein alpha (aSNAP), regulates epithelial junctions. aSNAP was enriched at apical junctions in SK-CO15 and T84 colonic epithelial cells and in normal human intestinal mucosa. siRNA- mediated knockdown of aSNAP inhibited AJ/TJ assembly and establishment of the paracellular barrier in SK-CO15 cells, which was accompanied by a significant down-regulation of p120-catenin and E-cadherin expression. A selective depletion of p120 catenin effectively disrupted AJ and TJ structure and compromised the epithelial barrier. However, overexpression of p120 catenin did not rescue the defects of junctional structure and permeability caused by aSNAP knockdown thereby suggesting the involvement of additional mechani