title: Rapid binding of synapsin I to F- and G-actin. A study using fluorescence resonance energy transfer.
abstract: Synapsin I is a nerve terminal phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent manner. By using fluorescence resonance energy transfer between purified components labeled with fluorescent probes, we now show that the binding of synapsin I to actin is a rapid phenomenon. Binding of synapsin I to actin can also be demonstrated when synaptic vesicles are present in the medium and appears to be modulated by ionic strength and synapsin I phosphorylation.
authors.affiliation: Dept. of Medical Pharmacology, University of Milan, Italy.
authors.forename: P E
authors.initials: PE
authors.lastname: Ceccaldi
authors.forename: F
authors.initials: F
authors.lastname: Benfenati
authors.forename: E
authors.initials: E
authors.lastname: Chieregatti
authors.forename: P
authors.initials: P
authors.lastname: Greengard
authors.forename: F
authors.initials: F
authors.lastname: Valtorta
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D013050:Spectrometry, Fluorescence; D016704:Synapsins / Q000378:metabolism*
chemical_list: D000199:Actins; D016704:Synapsins