How synapsin I may cluster synaptic vesicles |
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Authors: | Shupliakov Oleg Haucke Volker Pechstein Arndt |
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Institution: | aDepartment of Neuroscience, DBRM, Karolinska Institutet, 17177 Stockholm, Sweden;bDepartment of Membrane Biochemistry, Institute of Chemistry & Biochemistry, Freie Universität & Charité-Universitätsmedizin Berlin, 14195 Berlin, Germany;cLeibniz Institute of Molecular Pharmacology, Berlin-Buch, Germany |
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Abstract: | Synapsin I is the most abundant brain phosphoprotein present in conventional synapses of the CNS. Knockout and rescue experiments have demonstrated that synapsin is essential for clustering of synaptic vesicles (SVs) at active zones and the organization of the reserve pool of SVs. However, in spite of intense efforts it remains largely unknown how exactly synapsin I performs this function. It has been proposed that synapsin I in its dephosphorylated state may tether SVs to actin filaments within the cluster from where SVs are released in response to activity-induced synapsin phosphorylation. Recent studies, however, have failed to detect actin filaments inside the vesicle cluster at resting central synapses. Instead, proteins with established functional roles in SV recycling have been found within this presynaptic compartment. Here we discuss potential alternative mechanisms of synapsin I-dependent SV clustering in the reserve pool. |
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Keywords: | Synapse Synaptic vesicle Synapsin Vesicle clustering Endocytic proteins |
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