The proteome of different synaptic vesicle populations

Synaptic vesicles (SVs) are storage organelles for neurotransmitters in neurons. When an action potential arrives in the nerve terminal, voltage-gated calcium channels open and SVs undergo rapid exocytosis, releasing their neurotransmitter content into the synaptic cleft. The SV membrane is being rapidly retrieved by endocytosis and reutilized for the reformation of SVs. The SV cycle shares basic properties with other intracellular membrane pathways. Hence, not only can SVs be considered as the basic minimal units of synaptic transmission but also the basic minimal units of membrane transport, whose integral protein composition serves as the basis for all the functions a trafficking vesicle must perform. The high abundance and homogeneity obtained from purified SVs make them an ideal model for improving membrane based proteomics in addition to identifying novel SV proteins. In collaboration with Reinhard Jahn (Max Planck Institute for Biophysical Chemistry, Department of Molecular Neurobiology) we investigate the proteome of SVs (Link 1, Link 2),compare different SV populations and decipher post-translational modification in SV proteins.

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