Upon binding, a "closed" conformation is adopted, where C-terminal domains (C2F, C2G) rearrange. 3. Key Findings in Synaptic Transmission Ca 2+raised to the 2 plus power
Sensing: The C2D domain is identified as critical, as disruptions in this area alter synaptic sound encoding.
This molecular mechanism allows the ear to convert sound into neural signals at incredibly high speeds. tm,cc,jp
Lack of functional otoferlin or its C2 domain interaction prevents proper vesicle docking, leading to profound deafness. Summary Table: Otoferlin C2 Interactions Function/Location C2B-C2G Main interface for membrane binding C2D Crucial Ca 2+raised to the 2 plus power binding site; mutations affect sound encoding C2F-C2G Rearrange upon membrane binding to close structure Target Membrane Membrane where vesicles are docked
Binding Sites: High-resolution structures revealed that multiple Ca 2+raised to the 2 plus power Upon binding, a "closed" conformation is adopted, where
The protein utilizes C2 domains to bridge synaptic vesicles to the plasma membrane (plasma membrane being the "target membrane").
The binding requires cooperation between multiple C2 domains to secure the vesicle to the target membrane. This molecular mechanism allows the ear to convert
Based on the 2025 research regarding the protein , which is crucial for hearing and synaptic transmission,