Receptor-induced beta gamma release from fatty acylation-deficient mutants of G alpha z.

The neuronal-specific G protein Gz is known to interact with a large variety of receptors for neurotransmitters and hormones. Fatty acylations on the N-terminus of the alpha subunit of Gz (alpha z) provide anchorage to the plasma membrane. Fatty acylation-deficient mutants of alpha z have previously been shown to exhibit altered signaling properties. Since the N-terminus of alpha z is likely to play a critical role in beta gamma binding, we examined the ability of these mutants to interact with beta gamma subunits by means of receptor-mediated stimulation of beta gamma-sensitive type II adenylyl cyclase. Our results indicate that lack of myristoylation, but not lack of palmitoylation, impaired the ability of alpha z to mediate receptor-induced release of beta gamma subunits.