AMPA receptors modulate the reorganization of F-actin in Bergmann glia cells through the activation of RhoA
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Alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid glutamate receptors have been shown to modulate the morphology of the lamelar processes of Bergmann glia cells in the molecular layer of the cerebellum. Here we suggest that reorganization of F-actin may underlay the changes in the morphology of the lamelar processes. Using the fluorescent staining of F-actin with Phalloidin and the quantification of RhoA activation through immunoprecipitation or pull-down assays, we show that RhoA is activated after stimulation of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptors and leads to the reorganization of the actin cytoskeleton of Bergmann fibers. This reorganization of the actin cytoskeleton is reflected in the form of an increase in the intensity of the F-actin staining as well as in the loss of the number of Bergmann fibers stained with Phalloidin. Moreover, using a pharmacological approach, we show that activation of RhoA and the change in the intensity of the F-actin staining depends on the activation of PI3-K, focal adhesion kinase, and protein kinase C, whereas changes in the number of Bergmann fibers depend on external calcium in a RhoA independent manner. Our findings show that glutamate may induce a form of structural plasticity in Bergmann glia cells through the reorganization of the actin cytoskeleton. This may have implications in the way the synaptic transmission is processed in the cerebellum. (Figure presented.). © 2018 International Society for Neurochemistry
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actin; Bergmann glia; cytoskeletal reorganization; glutamate; RhoA alpha amino 3 hydroxy 5 methylisoxazole 4 propionic acid receptor; AMPA receptor; F actin; focal adhesion kinase; glutamic acid; phalloidin; phosphatidylinositol 3 kinase; propionic acid; protein kinase C; RhoA guanine nucleotide binding protein; unclassified drug; actin; AMPA receptor; glutamic acid; RhoA guanine nucleotide binding protein; RhoA protein, mouse; actin filament; adult; animal experiment; animal tissue; Article; Bergmann glia cell; cell plasticity; cerebellum; controlled study; enzyme activation; immunoprecipitation; limit of quantitation; male; mouse; nonhuman; priority journal; protein function; synaptic transmission; Western blotting; animal; Bagg albino mouse; glia; metabolism; physiology; signal transduction; Actin Cytoskeleton; Actins; Animals; Cerebellum; Glutamic Acid; Male; Mice; Mice, Inbred BALB C; Neuroglia; Receptors, AMPA; rhoA GTP-Binding Protein; Signal Transduction
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