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10.1074/jbc.RA117.001547

http://scihub22266oqcxt.onion/10.1074/jbc.RA117.001547
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C5971468!5971468!29615494
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suck abstract from ncbi


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pmid29615494      J+Biol+Chem 2018 ; 293 (21): 8217-29
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  • Small molecules that inhibit the late stage of Munc13-4?dependent secretory granule exocytosis in mast cells #MMPMID29615494
  • Bruinsma S; James DJ; Quintana Serrano M; Esquibel J; Woo SS; Kielar-Grevstad E; Crummy E; Qurashi R; Kowalchyk JA; Martin TFJ
  • J Biol Chem 2018[May]; 293 (21): 8217-29 PMID29615494show ga
  • Ca2+-dependent secretory granule fusion with the plasma membrane is the final step for the exocytic release of inflammatory mediators, neuropeptides, and peptide hormones. Secretory cells use a similar protein machinery at late steps in the regulated secretory pathway, employing protein isoforms from the Rab, Sec1/Munc18, Munc13/CAPS, SNARE, and synaptotagmin protein families. However, no small-molecule inhibitors of secretory granule exocytosis that target these proteins are currently available but could have clinical utility. Here we utilized a high-throughput screen of a 25,000-compound library that identified 129 small-molecule inhibitors of Ca2+-triggered secretory granule exocytosis in RBL-2H3 mast cells. These inhibitors broadly fell into six different chemical classes, and follow-up permeable cell and liposome fusion assays identified the target for one class of these inhibitors. A family of 2-aminobenzothiazoles (termed benzothiazole exocytosis inhibitors or bexins) was found to inhibit mast cell secretory granule fusion by acting on a Ca2+-dependent, C2 domain?containing priming factor, Munc13-4. Our findings further indicated that bexins interfere with Munc13-4?membrane interactions and thereby inhibit Munc13-4?dependent membrane fusion. We conclude that bexins represent a class of specific secretory pathway inhibitors with potential as therapeutic agents.
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