Complexins: Cytosolic proteins that regulate SNAP receptor function

@article{McMahon1995ComplexinsCP,
  title={Complexins: Cytosolic proteins that regulate SNAP receptor function},
  author={Harvey T. McMahon and Markus Missler and Cai Li and Thomas C. S{\"u}dhof},
  journal={Cell},
  year={1995},
  volume={83},
  pages={111-119}
}
A family of proteins called complexins was discovered that compete with alpha-SNAP, but not synaptotagmin, for SNAP receptor binding. Complexins I and II are highly homologous hydrophilic proteins that are tightly conserved, with 100% identity among mouse, rat, and human complexin II. They are enriched in neurons where they colocalize with syntaxin and SNAP-25; in addition, complexin II is expressed ubiquitously at low levels. Complexins bind weakly to syntaxin alone and not at all to… Expand
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TLDR
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Selective Interaction of Complexin with the Neuronal SNARE Complex
TLDR
It is concluded that complexins are specific ligands of the neuronal core complex that bind with a central α-helical domain, probably to the middle of the surface groove formed by synaptobrevin and syntaxin, and may regulate the function of ternary complexes and control membrane fusion through this interaction. Expand
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TLDR
This work shows that both synaptotagmins I and II, the two major neuronal isoforms, can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25) dimer, the immediate precursor of the soluble NSF attachment protein receptor (SNARE) fusion complex. Expand
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TLDR
Overexpression of Spring or its SNAP-25-interacting domain reduces Ca2+-dependent exocytosis from PC12 cells, indicating that Spring may act as a regulator of synaptic vesicle exocyTosis by controlling the availability of SNAP- 25 for the SNARE complex formation. Expand
Action of Complexin on SNARE Complex*
TLDR
It is proposed that complexin facilitates neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion. Expand
Direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1
TLDR
This work shows that synaphin directly binds to synaptotagmin 1, a major Ca2+ sensor for fast neurotransmitter release, in a 1:1 stoichiometry and suggests that the C-terminal region is essential for the interaction between these two proteins. Expand
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Electrophysiological recordings in the mutant hippocampus showed that ordinary synaptic transmission and paired‐pulse facilitation, a form of short‐term synaptic plasticity, were normal, however, long‐term potentiation in both CA1 and CA3 regions was impaired, suggesting that complexin II may not be essential for synaptic vesicle exocytosis, but it does have a role in the establishment of hippocampal LTP. Expand
Reinvestigation of the Role of Snapin in Neurotransmitter Release*
TLDR
It is concluded that the postulated role of snapin as a SNARE regulator in neurotransmitter release needs reconsideration, leaving the true function of this evolutionarily conserved protein to be discovered. Expand
Differential Phosphorylation of Syntaxin and Synaptosome‐Associated Protein of 25 kDa (SNAP‐25) Isoforms
TLDR
Investigating the ability of syntaxin and SNAP‐25 isoforms to serve as substrates for a variety of serine/threonine protein kinases suggests that although phosphorylation does not directly regulate the assembly of the synaptic SNARE complex, it may serve to modulateSNARE complex function through other proteins, including synaptotagmin I. Expand
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