Interaction of free and synaptic vesicle-bound synapsin I with F-actin

Fabio Benfenati, Flavia Valtorta, Evelina Chieregatti, Paul Greengard

Research output: Contribution to journalArticlepeer-review

Abstract

Synapsin 1 is a neuron-specific phosphoprotein that binds to small synaptic vesicles and F-actin in a phosphorylation-dependent fashion. We have found that dephosphorylated synapsin I induces a dose-dependent increase in the number of actin filaments, which at high ionic strength is abolished by synapsin I phosphorylation. The increase in filament number appears to be due to a nucleating effect of synapsin I and not to a barbed-end capping/severing activity. Synaptic vesicle-bound synapsin I was as effective as free synapsin 1 in increasing the number of filaments. These data support the view that synapsin I is involved in the regulation of the dynamics of the actin-based network during the exo-endocytotic cycle.

Original languageEnglish
Pages (from-to)377-386
Number of pages10
JournalNeuron
Volume8
Issue number2
DOIs
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Neuroscience(all)

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