G protein beta1gamma2 subunits promote microtubule assembly.

alpha and betagamma subunits of G proteins are thought to transduce signals from cell surface receptors to intracellular effector molecules. Galpha and Gbetagamma have also been implicated in cell growth and differentiation, perhaps due to their association with cytoskeletal components. In this report Gbetagamma is shown to modulate the cytoskeleton by regulation of microtubule assembly. Specificity among betagamma species exists, as beta1gamma2 stimulates microtubule assembly, and beta1gamma1 is without any effect. Furthermore, a mutant beta1gamma2, beta1gamma2(C68S), which does not undergo prenylation and subsequent carboxyl-terminal processing on the gamma subunit, does not stimulate the formation of microtubules. beta immunoreactivity was detected exclusively in the microtubule fraction after assembly in the presence of beta1gamma2, suggesting a preferential association with microtubules rather than soluble tubulin. Crude microtubule fractions from ovine brain contain Gbetagamma, and electron microscopy reveals a specific association with microtubules. The decoration of microtubules by Gbetagamma appears to be strikingly similar to the periodic pattern observed for microtubule-associated proteins, suggesting a similar site of activation of microtubule assembly by both agents. It is suggested that reformation of the cytoskeleton represents an additional cellular process mediated by Gbetagamma.