The chaperone protein smggds interacts with small gtpases entering the prenylation pathway by recognizing the last amino acid in the CAAX motif

Background: SmgGDS-607 and SmgGDS-558 regulate GTPase movement through the prenylation pathway. Results: The specificity of SmgGDS for GTPases depends on the GTPase CAAX sequence and the cellular context. Conclusion: SmgGDS-607 binds to nonprenylated GTPases that end in a leucine and enter the geranylgeranylation pathway. Significance: The identification of SmgGDS-607 as a novel CAAX-binding protein will accelerate the development of more effective cancer therapeutics.