| First Author | Hagemann A | Year | 2017 |
| Journal | FEBS Lett | Volume | 591 |
| Issue | 21 | Pages | 3637-3648 |
| PubMed ID | 28948621 | Mgi Jnum | J:354410 |
| Mgi Id | MGI:7734804 | Doi | 10.1002/1873-3468.12862 |
| Citation | Hagemann A, et al. (2017) Exploring the putative self-binding property of the human farnesyltransferase alpha-subunit. FEBS Lett 591(21):3637-3648 |
| abstractText | Farnesylation is an important post-translational protein modification in eukaryotes. Farnesylation is performed by protein farnesyltransferase, a heterodimer composed of an alpha- (FTalpha) and a beta-subunit. Recently, homodimerization of truncated rat and yeast FTalpha has been detected, suggesting a new role for FTalpha homodimers in signal transduction. We investigated the putative dimerization behaviour of human and rat FTalpha. 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. |
