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Actin polymerization regulates clathrin coat maturation during early stages of synaptic vesicle recycling at lamprey synapses
Author(s) -
Bourne Jennifer,
Morgan Jennifer R.,
Pieribone Vincent A.
Publication year - 2006
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/cne.21006
Subject(s) - actin remodeling of neurons , biology , microbiology and biotechnology , clathrin , synaptic vesicle , endocytic cycle , synaptic vesicle recycling , actin , actin remodeling , dendritic spine , lamprey , synapse , actin cytoskeleton , vesicle , neuroscience , cytoskeleton , biochemistry , endocytosis , membrane , receptor , fishery , cell , hippocampal formation
Although it is established that presynaptic actin participates in synaptic vesicle recycling at several synapses, the earliest stages at which actin polymerization is employed during this process are still unclear. To address this, we prevented actin polymerization at lamprey synapses by applying latrunculin B or swinholide A. Latrunculin and swinholide depolymerize actin by sequestering actin monomers and, in addition, swinholide can sever existing actin filaments. When injected into individual presynaptic axons of the intact spinal cord, fluorescently labeled monomeric actin rapidly incorporated in a calcium‐dependent manner into a stable, filamentous actin network concentrated at endocytic zones. This pool of actin was disrupted completely by latrunculin. At stimulated synapses, specific disruption of actin polymerization with latrunculin and swinholide induced a selective increase in unconstricted clathrin‐coated pits and, in the case of swinholide, an additional increase in the size of plasma membrane evaginations. These results indicate that actin polymerization participates initially in the maturation of clathrin‐coated pits during early stages of synaptic vesicle recycling. J. Comp. Neurol. 497:600–609, 2006. © 2006 Wiley‐Liss, Inc.