Topic
Complexin
About: Complexin is a research topic. Over the lifetime, 264 publications have been published within this topic receiving 19498 citations. The topic is also known as: IPR008849 & Complexin.
Papers published on a yearly basis
Papers
TL;DR: The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion and are spectacularly apparent in the exquisite speed and precision of synaptic exocytosis.
Abstract: The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion. Vesicular and target membrane-localized SNARE proteins zipper up into an alpha-helical bundle that pulls the two membranes tightly together to exert the force required for fusion. SM proteins, shaped like clasps, bind to trans-SNARE complexes to direct their fusogenic action. Individual fusion reactions are executed by distinct combinations of SNARE and SM proteins to ensure specificity, and are controlled by regulators that embed the SM-SNARE fusion machinery into a physiological context. This regulation is spectacularly apparent in the exquisite speed and precision of synaptic exocytosis, where synaptotagmin (the calcium-ion sensor for fusion) cooperates with complexin (the clamp activator) to control the precisely timed release of neurotransmitters that initiates synaptic transmission and underlies brain function.
2,102 citations
TL;DR: It is reported that in the absence of SNAP and NSF, these three SNAREs form a stable complex that can also bind synaptotagmin, suggesting that synapttagmin operates as a "clamp" to prevent fusion from proceeding in the absent of a signal.
2,016 citations
TL;DR: It is proposed that synaptotagmin I is the major low affinity Ca2+ sensor mediating Ca2-regulation of synchronous neurotransmitter release in hippocampal neurons and not essential for asynchronous or Ca(2+)-independent release.
1,571 citations
TL;DR: This work has shown that direct flow of Ca(2+) ions from Ca( 2+) channels to synaptotagmin, which then triggers fusion, thus mediating tight millisecond coupling of an action potential to neurotransmitter release.
1,149 citations
TL;DR: A point mutation in synaptotagmin I is studied that causes a twofold decrease in overall Ca2+ affinity without inducing structural or conformational changes and participates in triggering neurotransmitter release at the synapse.
Abstract: In all synapses, Ca2+ triggers neurotransmitter release to initiate signal transmission. Ca2+ presumably acts by activating synaptic Ca2+ sensors, but the nature of these sensors--which are the gatekeepers to neurotransmission--remains unclear. One of the candidate Ca2+ sensors in release is the synaptic Ca2+-binding protein synaptotagmin I. Here we have studied a point mutation in synaptotagmin I that causes a twofold decrease in overall Ca2+ affinity without inducing structural or conformational changes. When introduced by homologous recombination into the endogenous synaptotagmin I gene in mice, this point mutation decreases the Ca2+ sensitivity of neurotransmitter release twofold, but does not alter spontaneous release or the size of the readily releasable pool of neurotransmitters. Therefore, Ca2+ binding to synaptotagmin I participates in triggering neurotransmitter release at the synapse.
1,036 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 8 |
| 2020 | 6 |
| 2019 | 12 |
| 2018 | 19 |
| 2017 | 13 |
| 2016 | 13 |