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Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2008 Oct 27;66(3):460. doi: 10.1007/s00018-008-8372-z

Progress in understanding the neuronal SNARE function and its regulation

T-Y Yoon 1,, Y-K Shin 2,
PMCID: PMC11131560  PMID: 18953690

Abstract.

Vesicle budding and fusion underlies many essential biochemical deliveries in eukaryotic cells, and its core fusion machinery is thought to be built on one protein family named soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE). Recent technical advances based on site-directed fluorescence labelling and nano-scale detection down to the single-molecule level rapidly unveiled the protein and the lipid intermediates along the fusion pathway as well as the molecular actions of fusion effectors. Here we summarize these new exciting findings in context with a new mechanistic model that reconciles two existing fusion models: the proteinaceous pore model and the hemifusion model. Further, we attempt to locate the points of action for the fusion effectors along the fusion pathway and to delineate the energetic interplay between the SNARE complexes and the fusion effectors.

Keywords. Membrane fusion, SNARE, neurotransmitter release, synaptotagmin 1, single molecule study, complexin

Footnotes

Received 01 July 2008; received after revision 29 August 2008; accepted 23 September 2008

Contributor Information

T.-Y. Yoon, FAX: +82-42-350-2510, Email: tyyoon@kaist.ac.kr

Y.-K. Shin, FAX: +1-515-294-0453, Email: colishin@iastate.edu


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

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