| Abstract: | It was found that about 30% of the alpha-subunit of the bovine brain GTP-binding protein, Go, is bound to the cytoskeleton. The efficiency of Go alpha binding to the cytoskeleton components depends on the nature of the guanyl nucleotides GDP-beta-S, Gpp (NH) p] present in the incubation medium. It was shown that the alpha-subunit interaction with cytoskeleton components is controlled by ATP-dependent reactions. ATP diminishes the degree Go alpha adsorption. The non-hydrolysable ATP analog, App (NH) p, has no effect on the Go alpha interaction with the cytoskeleton. It was found that one of the cytoskeleton components capably of binding to Go alpha is tubulin. Similar interactions were detected in human neuroblastoma N2A cells. |
