Synaptic Vesicle Fusion and SNARE Complexes
Overview of Synaptic Vesicle Fusion Mechanisms
Key Proteins Involved in Fusion
SNAP-25, Synaptobrevin, Syntaxin
These proteins are critical in forming the SNARE complex which is essential for synaptic vesicle fusion.
They facilitate the priming of vesicles, making them fusion competent.
Priming and SNARE Complex Assembly
Fusion Competence of Primed Vesicles
Primed vesicles are those that are ready to fuse with the presynaptic membrane, however, they have a challenge: syntaxin is usually in a default closed configuration, hiding the SNARE binding domain that is necessary for fusion.
SNARE Complex Formation
To achieve priming, assembly of the SNARE complex is required, involving syntaxin, synaptobrevin, and SNAP-25.
Closed syntaxin cannot form the SNARE complex, so understanding how to transition to an open state is crucial.
Syntaxin Configurations
Closed versus Open State of Syntaxin
Closed Syntaxin
Hinders SNARE complex formation.
Open Syntaxin
Allows for SNARE complex assembly with synaptobrevin and SNAP-25.
Role of UNC-13
UNC-13 Functionality
UNC-13 binds to the N-terminus of syntaxin, promoting the assembly of the SNARE complex.
This interaction is crucial for transitioning syntaxin from the closed to the open state, facilitating vesicle docking.
Docking of Synaptic Vesicles
Docking Mechanism
SNARE complex assembly brings the synaptic vesicle into close proximity with the presynaptic membrane, enabling docking.
Mutations in syntaxin or UNC-13 result in defects in synaptic vesicle docking.
High-Pressure Freezing Technique
Utilized to preserve synapses in a physiological state for examination of docked and undocked vesicles.
Imaging and Structural Insights
High-Resolution Imaging
Visual representation of the symmetrical organization of protein complexes anchoring vesicles to the plasma membrane.
Images include various orientations (side view, top view) with scale indicated (e.g., 50 nm).
Crystal Structure and Regulation by Calcium
Munc13/UNC-13 Crystal Structure
Discovered conformations regulated by diacylglycerol (DAG) and calcium ions (Ca2+).
States of Munc13
State 1: "Captured" with unassembled SNAREs.
State 2: "Pre-primed" with unassembled SNAREs.
State 3: "Primed" state with clamped SNARE pins.
Role of Calcium in Vesicle Fusion
Mechanism of Calcium Influx
Voltage-gated calcium channels open in response to action potentials, leading to calcium influx.
This calcium influx triggers vesicle fusion due to the close proximity of calcium channels to primed vesicles, typically occurring within 200 ms of influx.
Synaptotagmin's Role in Synaptic Release
Knockout Studies of Synaptotagmin I
Mice lacking synaptotagmin demonstrate a loss of synchronous release of neurotransmitters, indicating its crucial role in the process.
Control versus synaptotagmin knockout demonstrated the impact on release patterns.
Interaction Between Calcium and Synaptotagmin
Calcium Binding Interaction
Calcium interacts with the calcium-binding protein synaptotagmin, essential for vesicle fusion.
Synaptotagmin Structure and Mechanism
Ring Formation
Synaptotagmin forms rings around the synaptic vesicle to interact with SNARE complexes.
C2B Domain Role
Upon binding calcium, the C2B domain of synaptotagmin inserts into the plasma membrane, causing it to dimple, facilitating membrane fusion.
Process of Fusion Initiation
Calcium and SNARE Complex Mechanics
Synaptotagmin binds to the SNARE complex, holding it together until calcium presence triggers further interactions.
Calcium binding to the C2B domain results in C2B insertion into the target membrane, which changes membrane curvature, lowering the energy barrier for fusion.
Ultimately, calcium-synaptotagmin interactions drive the complete zipping of SNARE complexes to initiate fusion.
Summary of Exocytosis Process
Key Steps in Exocytosis
Munc13 promotes the docking of synaptic vesicles through SNARE complex assembly (priming).
Synaptotagmin clamps primed vesicles until a calcium signal is received.
Calcium channels open in response to action potentials, leading to synaptotagmin binding and consequent vesicle fusion.