Exploring the putative self-binding property of the human farnesyltransferase alpha-subunit

Farnesylation is an important post-translational protein modification in eukaryotes. Farnesylation is performed by protein farnesyltransferase, a heterodimer composed of an alpha- (FT alpha) and a beta-subunit. Recently, homodimerization of truncated rat and yeast FT alpha has been detected, suggesting a new role for FT alpha homodimers in signal transduction. We investigated the putative dimerization behaviour of human and rat FT alpha. Different in vitro and in vivo approaches revealed no self-dimerization and a presumably artificial formation of homotrimers and higher homo-oligomers in vitro. Our study contributes to the clarification of the physiological features of FTase in different species and may be important for the ongoing development of FTase inhibitors.