The
G proteins G S and Gi1 appear to be capable of binding to
tubulin specifically, and it has been suggested that such binding results in
G protein activation via direct transfer of
GTP. This study was undertaken to demonstrate that consequences of
G protein activation by
tubulin, i.e., stimulation or inhibition of
adenyl cyclase, were dependent on the
G proteins expressed as well as unique aspects of the membrane or cytoskeleton in a given cell type. Membranes from rat C6
glioma cells, which express
G s alpha but not G i alpha 1, responded to the addition of
tubulin with a stable activation of
adenyl cyclase. Conversely, membranes from rat cerebral cortex, which contain both G s and G i 1, responded to exogenous
tubulin with a stable inhibition of
adenyl cyclase. Unlike C6 membranes, cerebral cortex membranes are richly endowed with
tubulin, and antitubulin
antibodies immunoprecipitated complexes of
tubulin and G i 1 and G s from
detergent extracts of these membranes. Nearly 90% of the
G s alpha from
Triton X-114 extracts coimmunoprecipitated with
tubulin, suggesting that these
proteins exist as a complex in the synaptic membrane. Such complexes may provide the framework for a
G protein-cytoskeleton link that participates in the modulation of cellular signal transduction.