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Protein Translocation Machinery on the ER Membrane01:28

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Updated: Apr 15, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
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Re-visiting the trans insertion model for complexin clamping.

Shyam S Krishnakumar1, Feng Li1, Jeff Coleman1

  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, United States.

Elife
|April 3, 2015
PubMed
Summary
This summary is machine-generated.

Complexin acts as a clamp to regulate neurotransmitter release by cross-linking SNARE complexes. New biochemical data support this trans clamping model, refuting recent challenges.

Keywords:
biochemistrybiophysicscomplexinmembrane fusionneurotransmittersnonestructural biology

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Area of Science:

  • Molecular neuroscience
  • Biochemistry
  • Cellular biology

Background:

  • Complexin's role in regulating neurotransmitter release is debated.
  • Previous studies proposed a trans clamping model for complexin's function.
  • A recent NMR study questioned this model based on new data.

Purpose of the Study:

  • To re-evaluate the trans clamping model of complexin.
  • To present new biochemical evidence supporting complexin's clamp function.
  • To address the findings of a recent NMR study.

Main Methods:

  • Biochemical assays
  • Analysis of SNARE complex interactions
  • Re-interpretation of existing biophysical data

Main Results:

  • New biochemical data validate the trans interaction of complexin.
  • The trans insertion model for complexin clamping remains relevant.
  • Discrepancies with NMR study findings are addressed.

Conclusions:

  • The trans clamping mechanism of complexin is supported by new evidence.
  • Complexin plays a crucial role in regulating SNARE-mediated release.
  • Further research should consider the trans insertion model.