| Literature DB >> 1739463 |
F Benfenati1, F Valtorta, E Chieregatti, P Greengard.
Abstract
Synapsin I 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 I 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.Entities:
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Year: 1992 PMID: 1739463 DOI: 10.1016/0896-6273(92)90303-u
Source DB: PubMed Journal: Neuron ISSN: 0896-6273 Impact factor: 17.173