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First published online June 17, 2009

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Switching on syntaxins

Membrane fusion in all eukaryotes is regulated by SNARE complexes, which comprise a four-helical bundle of SNARE motifs. Syntaxins form part of this complex, and contain in their structure an N-terminal Habc domain in addition to a SNARE motif. It has been previously shown that some syntaxins exist in a closed conformation, in which the Habc domain binds intramolecularly to the SNARE motif, preventing the formation of SNARE complexes. However, whether this is a conserved feature of syntaxins has been a contentious issue. Now, Nia Bryant and colleagues (p. 2292) show that mammalian syntaxin 16 (Sx16) is a functional homologue of yeast Tlg2p, and that these syntaxins are regulated in an evolutionarily conserved manner. More specifically, they show that the conserved Sec1p/Munc18 (SM) protein Vps45p regulates the assembly of SNARE complexes by relieving the inhibition mediated by the syntaxin Habc domain. Although more detailed structural data will be required to confirm the conformational changes of these proteins at the molecular level, this study indicates that SM proteins can facilitate the switch of syntaxins from a closed to an open conformation and thereby regulate SNARE-complex assembly.

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Related articles in JCS:

Functional homology of mammalian syntaxin 16 and yeast Tlg2p reveals a conserved regulatory mechanism

Marion S. Struthers, Scott G. Shanks, Chris MacDonald, Lindsay N. Carpp, Alicja M. Drozdowska, Dimitrios Kioumourtzoglou, Melonnie L. M. Furgason, Mary Munson, and Nia J. Bryant
JCS 2009 122: 2292-2299. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Social Bookmarking                         What's this?