{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,13]],"date-time":"2026-03-13T17:16:34Z","timestamp":1773422194639,"version":"3.50.1"},"reference-count":27,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2004,5,17]],"date-time":"2004-05-17T00:00:00Z","timestamp":1084752000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2004,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Synaptophysin is one of the most abundant membrane proteins of small synaptic vesicles. In mature nerve terminals it forms a complex with the vesicular membrane protein synaptobrevin, which appears to modulate synaptobrevin's interaction with the plasma membrane\u2010associated proteins syntaxin and SNAP25 to form the SNARE complex as a prerequisite for membrane fusion. Here we show that synaptobrevin is preferentially cleaved by tetanus toxin while bound to synaptophysin or when existing as a homodimer. The synaptophysin\/synaptobrevin complex is, however, not affected when neuronal secretion is blocked by botulinum A toxin which cleaves SNAP25. Excessive stimulation with \u03b1\u2010latrotoxin or Ca<jats:sup>2+<\/jats:sup>\u2010ionophores dissociates the synaptophysin\/synaptobrevin complex and increases the interaction of the other SNARE proteins. The stimulation\u2010induced dissociation of the synaptophysin\/synaptobrevin complex is not inhibited by pre\u2010incubating neurones with botulinum A toxin, but depends on extracellular calcium. However, the synaptophysin\/synaptobrevin complex cannot be directly dissociated by calcium alone or in combination with magnesium. The dissociation of synaptobrevin from synaptophysin appears to precede its interaction with the other SNARE proteins and does not depend on the final fusion event. This finding further supports the modulatory role the synaptophysin\/synaptobrevin complex may play in mature neurones.<\/jats:p>","DOI":"10.1111\/j.1471-4159.2004.02472.x","type":"journal-article","created":{"date-parts":[[2004,6,15]],"date-time":"2004-06-15T20:02:27Z","timestamp":1087329747000},"page":"1-8","source":"Crossref","is-referenced-by-count":38,"title":["The synaptophysin\/synaptobrevin complex dissociates independently of neuroexocytosis"],"prefix":"10.1111","volume":"90","author":[{"given":"Clemens","family":"Reisinger","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sowmya V.","family":"Yelamanchili","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Britta","family":"Hinz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Diana","family":"Mitter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anja","family":"Becher","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hans","family":"Bigalke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gudrun","family":"Ahnert\u2010Hilger","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,5,17]]},"reference":[{"key":"e_1_2_12_2_1","first-page":"1","article-title":"Synaptobrevin is essential for secretion but not for the development of synaptic processes","volume":"70","author":"Ahnert\u2010Hilger G.","year":"1996","journal-title":"Eur. 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