Recombinant Human Synapsin I protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Synapsin I also known as SYN1 plays an important role in synaptic function. It is a phosphoprotein with a molecular mass of approximately 78 kDa. Synapsin I is expressed mainly in the neurons of the central nervous system (CNS). It binds to synaptic vesicles and actin cytoskeleton which suggests that it functions in modulating neurotransmitter release at the presynaptic terminals. This modulation occurs as synapsin I undergoes phosphorylation which is critical for its activity.

Biological function summary

Synapsin I influences synaptic plasticity and is part of the synaptic vesicle trafficking complex. In its dephosphorylated state Synapsin I associates with synaptic vesicles anchoring them to the actin cytoskeleton. Upon phosphorylation Synapsin I changes conformation causing vesicles to mobilize. This activity supports the modulation of neurotransmitter release impacting learning and memory functions.

Pathways

Synapsin I participates significantly in the neurotransmitter release cycle and synaptic vesicle trafficking pathway. Protein kinase A (PKA) and Ca2+/calmodulin-dependent protein kinase II (CaMKII) regulate its phosphorylation affecting how Synapsin I contributes to vesicle release. The phosphorylation of Synapsin I at sites such as serine 9 enables its interaction with other proteins like actin and spectrin facilitating vesicle movement.

Altered Synapsin I expression associates with neurological conditions like epilepsy and schizophrenia. In epilepsy dysregulation of Synapsin I phosphorylation processes can result in imbalanced neurotransmitter release potentially leading to seizures. Its connection to schizophrenia involves changes in synaptic plasticity which neurotransmitter systems such as dopamine and related proteins like alpha-synuclein also influence. Understanding these interactions can aid in developing therapeutic strategies.