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Exocytotic fusion pores are composed of both lipids and proteins. | LitMetric

AI Article Synopsis

  • During exocytosis, fusion pores form to allow neurotransmitters and hormones to escape from secretory vesicles, with SNARE proteins playing a key role in this process.
  • Researchers used nanodiscs to study these fusion pores, finding that about two molecules of synaptobrevin 2 could efficiently facilitate the release of glutamate when stimulated by calcium ions.
  • The study revealed that different parts of SNARE proteins have unique functions in lipid mixing and content release, suggesting that fusion pores are made up of both lipids and proteins.

Article Abstract

During exocytosis, fusion pores form the first aqueous connection that allows escape of neurotransmitters and hormones from secretory vesicles. Although it is well established that SNARE proteins catalyze fusion, the structure and composition of fusion pores remain unknown. Here, we exploited the rigid framework and defined size of nanodiscs to interrogate the properties of reconstituted fusion pores, using the neurotransmitter glutamate as a content-mixing marker. Efficient Ca(2+)-stimulated bilayer fusion, and glutamate release, occurred with approximately two molecules of mouse synaptobrevin 2 reconstituted into ∼6-nm nanodiscs. The transmembrane domains of SNARE proteins assumed distinct roles in lipid mixing versus content release and were exposed to polar solvent during fusion. Additionally, tryptophan substitutions at specific positions in these transmembrane domains decreased glutamate flux. Together, these findings indicate that the fusion pore is a hybrid structure composed of both lipids and proteins.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4756907PMC
http://dx.doi.org/10.1038/nsmb.3141DOI Listing

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