Changes in mobility of synaptic vesicles with assembly and disassembly of actin network.
In a presynaptic terminal, neurotransmitters are stored in synaptic vesicles and secreted into the synaptic cleft as a final step of cell signal transduction. At a static state, the vesicles are retained in the highly dense actin network. Prior to exocytosis, the dense actin network must disassemble or largely be organized. Actin networks are formed in vitro which retain synaptic vesicles prepared from rat cerebral cortex. Dynamic behaviors of synaptic vesicles are measured by the dynamic light scattering method. The D(app) values of synaptic vesicles confined in actin network became less than 1/4 those of free vesicles. The motions of synaptic vesicles are substantially restricted. This means that synaptic vesicles which are liberated from the actin network by detachment of synapsin 1 molecules are still trapped in the cage-like space of actin filaments. The actin network is disassembled by the actin severing protein, gelsolin, which is activated in the presence of microM level free Ca2+ ions. The D(app)(v) values of synaptic vesicles after severing the actin network return to those of free vesicles in the presence of short actin fragments. A molecular model for exocytosis in the synaptic terminal is constructed on the basis of these results.
Miyamoto
S
S
Department of Biochemical Engineering, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Fukuoka, Japan.
D008841:Actin Cytoskeleton / Q000502:physiology*; D000199:Actins / Q000502:physiology*; D000818:Animals; D001921:Brain / Q000648:ultrastructure; D004058:Diffusion; D018260:Gelsolin / Q000494:pharmacology; D008027:Light; D009038:Motion; D011817:Rabbits; D051381:Rats; D012542:Scattering, Radiation; D013572:Synaptic Vesicles / Q000502:physiology*
D000199:Actins; D018260:Gelsolin