{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T15:00:30Z","timestamp":1776351630496,"version":"3.51.2"},"reference-count":42,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2012,1,9]],"date-time":"2012-01-09T00:00:00Z","timestamp":1326067200000},"content-version":"vor","delay-in-days":1714,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biology of the Cell"],"published-print":{"date-parts":[[2007,5]]},"abstract":"<jats:p><jats:italic>Background information<\/jats:italic>. TI\u2010VAMP (tetanus neurotoxin\u2010insensitive vesicle\u2010associated membrane protein; also called VAMP7) belongs to the Longin subfamily of v\u2010SNAREs (vesicular soluble <jats:italic>N<\/jats:italic>\u2010ethylmaleimide\u2010sensitive fusion protein\u2010attachment protein receptors). The regulatory N\u2010terminal extension, called the Longin domain, of TI\u2010VAMP has been shown previously to have a dual biochemical function: it inhibits the capacity of TI\u2010VAMP to form SNARE complexes and it binds to the \u03b4 subunit of the AP\u20103 (adaptor protein 3) complex in early endosomes, thereby targeting TI\u2010VAMP to late endosomes.<\/jats:p><jats:p><jats:italic>Results<\/jats:italic>. We have generated MDCK (Madin\u2014Darby canine kidney) cell lines expressing the Longin domain of TI\u2010VAMP coupled to GFP (green fluorescent protein) in a doxycycline\u2010dependent manner. As expected, AP\u20103\u03b4 (AP\u20103 \u03b4 subunit) is not properly localized in Longin\u2010expressing cells. We have shown that the expression of the Longin domain impairs lysosomal secretion, as determined by the release of a pre\u2010internalized fluorescent fluid\u2010phase marker and by electron microscopy of the membrane\u2010associated released particles. Membrane repair following mechanical wounding, a process requiring lysosomal secretion, is also impaired in cells expressing the Longin domain. Furthermore, cell migration, assessed by wound healing of MDCK monolayers, is also inhibited.<\/jats:p><jats:p><jats:italic>Conclusions<\/jats:italic>. The results of the present study suggest that the expression of the Longin domain of TI\u2010VAMP regulates lysosomal secretion of epithelial cells and provide molecular evidence for a role of the late endocytic system in cell migration.<\/jats:p>","DOI":"10.1042\/bc20060097","type":"journal-article","created":{"date-parts":[[2007,4,19]],"date-time":"2007-04-19T09:11:33Z","timestamp":1176973893000},"page":"261-271","source":"Crossref","is-referenced-by-count":81,"title":["Expression of the Longin domain of TI\u2010VAMP impairs lysosomal secretion and epithelial cell 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