Synaptotagmin I is characterized by:
The C2 domains are essential for calcium binding, which is a critical function of synaptotagmin I. When calcium ions bind to these domains, synaptotagmin I acts as a calcium sensor, triggering the release of neurotransmitters by facilitating the fusion of synaptic vesicles with the presynaptic membrane .
Synaptotagmin I is integral to the neurotransmitter release cycle. It senses calcium ion concentrations as low as 10 parts per million (ppm) and signals the SNARE complex to open fusion pores, allowing neurotransmitters to be released into the synaptic cleft . This process is vital for synaptic transmission and communication between neurons.
Recombinant Synaptotagmin I is produced using recombinant DNA technology, which involves inserting the SYT1 gene into a suitable expression system, such as bacteria or mammalian cells. This allows for the production of large quantities of the protein for research and therapeutic purposes.
Recombinant Synaptotagmin I is used in various studies to understand its role in neurotransmitter release and its potential implications in neurological disorders. It is also used in drug development and screening for compounds that can modulate its activity.