This molecular mechanism allows the ear to convert sound into neural signals at incredibly high speeds.
The protein utilizes several C2 domains (C2A-C2F) to bind Ca 2+raised to the 2 plus power and lipids, as shown in the protein structure below. 2. C2 Domains: Function & Interactions
Based on the 2025 research regarding the protein , which is crucial for hearing and synaptic transmission, tm,cc,jp
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
This guide focuses on the molecular mechanism of otoferlin-mediated vesicle docking and Ca 2+raised to the 2 plus power sensing in inner hair cells (IHCs). Role: Otoferlin acts as a key Ca 2+raised to the 2 plus power sensor for synaptic vesicle fusion in auditory IHCs. This molecular mechanism allows the ear to convert
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
The study highlights that membrane binding involves a cooperative effort of multiple domains. C2 Domains: Function & Interactions Based on the
Sensing: The C2D domain is identified as critical, as disruptions in this area alter synaptic sound encoding.