Receptor-induced βγ release from fatty acylation-deficient mutants of Gαz

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Abstract
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 α subunit of Gz (αz) provide anchorage to the plasma membrane. Fatty acylation-deficient mutants of αz have previously been shown to exhibit altered signaling properties. Since the N-terminus of αz is likely to play a critical role in βγ binding, we examined the ability of these mutants to interact with βγ subunits by means of receptor-mediated stimulation of βγ-sensitive type II adenylyl cyclase. Our results indicate that lack of myristoylation, but not lack of palmitoylation, impaired the ability of αz to mediate receptor-induced release of βγ subunits.