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J. Biol. Chem., Vol. 266, Issue 33, 22242-22245, 11, 1991
J Kirsch, D Langosch, P Prior, UZ Littauer, B Schmitt and H Betz
Abteilung Neurochemie, Max-Planck-Institut fur Hirnforschung, Frankfurt, Germany.
A peripheral membrane protein with a relative molecular mass of 93,000 Da is associated with cytoplasmic domains of the inhibitory glycine receptor of mammalian spinal cord. Here, evidence is given that this 93- kDa protein binds to polymerized tubulin. First, tubulin cofractionated with the 93-kDa protein upon affinity purification of the glycine receptor. Second, tubulin bound to the isolated 93-kDa protein in an overlay procedure. Third, in assays containing the purified glycine receptor, the 93-kDa protein as well as the glycine receptor alpha and beta subunits coassembled with tubulin and microtubules. The interaction of the 93-kDa protein with tubulin displayed high affinity (KD approximately 2.5 nM) and significant cooperativity (Hill coefficient approximately 2.1) and approached a stoichiometry of approximately 1:4 under saturating conditions. These data suggest that the 93-kDa protein anchors the glycine receptor at postsynaptic sites via binding to subsynaptic tubulin.
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