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Deconstructing complexin function in activating and clamping Ca2+-triggered exocytosis by comparing knockout and

Xiaofei Yang1, Peng Cao, Thomas C Südhof

  • 1Department of Molecular and Cellular Physiology and Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305.

Proceedings of the National Academy of Sciences of the United States of America
|December 4, 2013
PubMed
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Complexin proteins are crucial for vesicle release and spontaneous exocytosis. This study clarifies their varied roles in neuronal function, highlighting differences between knockdown and knockout models.

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SNARE proteinmembrane fusionneurotransmitter releasesynaptic transmissionsynaptotagmin

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Complexins are presynaptic proteins that bind SNARE complexes and are known to regulate neurotransmitter release.
  • Previous studies on complexin function in exocytosis yielded conflicting results, particularly regarding spontaneous exocytosis and the readily releasable pool (RRP).
  • Discrepancies in findings between complexin knockdown (DKD) and knockout (DKO) models necessitate direct comparison to elucidate complexin's precise roles.

Purpose of the Study:

  • To directly compare the functional consequences of complexin double knockdown (DKD) and double knockout (DKO) in different neuronal preparations.
  • To clarify the distinct roles of complexins in vesicle priming, spontaneous exocytosis, and Ca(2+)-triggered exocytosis.
  • To investigate the compensatory mechanisms and the influence of specific complexin isoforms and their localization on neuronal function.

Main Methods:

  • Comparison of complexin DKD and DKO phenotypes in cultured cortical and olfactory bulb neurons.
  • Assessment of vesicle priming and spontaneous exocytosis rates in genetically modified neurons.
  • Analysis of complexin mRNA expression levels and functional effects of complexin isoform overexpression.
  • Investigation of the role of the C-terminal lipid anchor in complexin function.

Main Results:

  • Complexin-deficient neurons (DKD and DKO) consistently showed a ~50% reduction in vesicle priming.
  • Complexin DKD increased spontaneous exocytosis, while DKO's effect varied by neuronal type (cortical vs. olfactory bulb).
  • Complexin DKD, but not DKO, induced compensatory increases in complexin-3 and -4 mRNA. Complexin-3, but not complexin-1, increased spontaneous exocytosis, an effect mimicked by lipid-anchored complexin-1.

Conclusions:

  • Complexins are essential for vesicle priming and Ca(2+)-triggered exocytosis.
  • Complexins modulate spontaneous exocytosis, with effects dependent on neuronal developmental history and subcellular localization.
  • Complexin isoforms exhibit distinct regulatory functions in exocytosis, influenced by post-translational modifications like lipid anchoring.