Ed Chapman and colleagues were recently published in Nature Communications for their work on message transfer regulation between mammal neurons. Specifically, Chapman describes a key component of the system — the “clamp” — that prevents the fusion pore from completing its formation and opening.
The fusion pore forms in synapses, the junctions between adjacent neurons. The pore, comprising “SNARE” proteins, cannot release a signal until calcium ions trigger the opening. The calcium sensor is a protein called synaptotagmin which, Chapman has now found, is also key to the fusion clamp. They found two candidate clamp molecules: complexin and a type of synaptotagmin called syt-1.
“Unexpectedly, we gained insights into a key question in synaptic neuroscience: since reconstituted SNARE proteins are constitutively active, what molecules clamp SNARE complexes to enable precisely timed control of SV fusion? Our results indicate that the C2B domain of syt1 corresponds to this long sought-after fusion clamp in mammalian nerve terminals.”
Read more information here: https://news.wisc.edu/clamp-regulates-message-transfer-between-mammal-neurons/
For Full paper, click here: Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin, Nature Communications, Volume 10, Article number: 4076 (2019) by Nicholas A. Courtney, Huan Bao, Joseph S. Briguglio & Edwin R. Chapman.