Re-visiting the trans insertion model for complexin clamping.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 25831964.
- Also identified by DOI 10.7554/eLife.04463 and PMC identifier 4384536.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
We have previously proposed that complexin cross-links multiple pre-fusion SNARE complexes via a trans interaction to function as a clamp on SNARE-mediated neurotransmitter release. A recent NMR study was unable to detect the trans clamping interaction of complexin and therefore questioned the previous interpretation of the fluorescence resonance energy transfer and isothermal titration calorimetry data on which the trans clamping model was originally based. Here we present new biochemical data that underscore the validity of our previous interpretation and the continued relevancy of the trans insertion model for complexin clamping.
Medical subject headings
- Adaptor Proteins, Vesicular Transport
- Nerve Tissue Proteins
- Neurons
- Synaptic Transmission