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Synopses of Research Articles A Flexible Syntaxin Solves the Mystery of the SNAREd Munc Richard Robinson | DOI: 10.1371/journal.pbio.0040359 Fusion of two plasma membranes is central to exocytosis, the process by which a cell secretes neurotransmitters, digestive enzymes, and other products. If you believe the simple diagrams in introductory biology textbooks, you’d think this fusion occurs as soon as two membranes touch. Not so—in fact, membrane fusion requires interaction among a complex set of proteins in the membranes, collectively termed SNARE proteins. SNAREs are assisted by a second group, called SM proteins, which bind to them and help promote their functions. Among the SM proteins, one, called Munc18-1, has stood out as something of an oddball. When the others bind to their respective SNAREs, they leave the SNAREs in an open conformation, available for interacting with others and forming the complexes that drive membrane fusion. In contrast, Munc18-1 appears to fold its SNARE, syntaxin 1, into a closed conformation, making it unavailable for binding to other SNAREs. But this result has been obtained only in membrane- free solutions, and the behavior of membrane-bound Munc18-1 has been a mystery. A new study by Felipe Zilly, Thorsten Lang, and colleagues resolves the mystery of the syntaxin–Munc18- 1 interaction and explains how their binding promotes interactions with other SNAREs. been shown that the addition of synaptobrevin drives syntaxin (without Munc18-1) in conjunction with SNAP-25 (the third SNARE essential for neuroexocytosis) into SNARE complexes. They reasoned that adding synaptobrevin to syntaxin–Munc18-1 would not drive syntaxin into SNARE complexes if syntaxin remained closed. Conversely, if syntaxin could partially open while bound to Munc18- 1, it would be able to interact with synaptobrevin and join the SNARE complex. And this is what they found—when synaptobrevin was added, syntaxin unhitched from Munc18-1 and joined the SNARE complex