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Journal of Neuroscience, Vol 15, 4148-4156, Copyright © 1995 by Society for Neuroscience
The postsynaptic localization of the glycine receptor-associated protein gephyrin is regulated by the cytoskeleton
J Kirsch and H Betz
Department of Neurochemistry, Max-Planck-Institute for Brain Research, Frankfurt/Main, Federal Republic of Germany.
The mechanisms underlying the postsynaptic localization of neurotransmitter
receptors are poorly understood. Recently, the peripheral membrane protein
gephyrin has been shown to be essential for the formation of inhibitory
glycine receptor clusters in cultured rat spinal cord neurons. In vitro
gephyrin binds with high affinity to polymerized tubulin. Here, the
interaction of gephyrin with different components of the cytoskeleton was
investigated in primary cultures of rat spinal neurons. After treatment
with alkaloids affecting the cytoskeleton, the morphology of post-synaptic
gephyrin clusters was analyzed by confocal immunofluorescence microscopy.
Depolymerization of microtubules by demecolcine reduced both the percentage
of cells with postsynaptic gephyrin clusters and the number of
clusters/cell. The size of the remaining gephyrin clusters was increased
whereas their gephyrin density was significantly lower than under control
conditions. Depolymerization of microfilaments by cytochalasin D in
contrast generated smaller clusters of increased gephyrin density.
Demecolcine also dispersed postsynaptic glycine receptor clusters as
revealed by immunostaining with a specific monoclonal antibody. These
findings support the view that in vivo gephyrin anchors receptor
polypeptides to the cytoskeleton by a complex interaction with microtubules
and microfilaments.
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