Exploring the putative self‐binding property of the human farnesyltransferase alpha‐subunit. Issue 21 (11th October 2017)

• Record Type: Journal Article
• Authors: Hagemann, Anna; Müller, Grit; Manthey, Iris; Bachmann, Hagen S.
• Is Part Of: FEBS letters. Volume 591:Issue 21(2017)
• Page Start: 3637
• Page End: 3648
• Publication Date: 2017-10-11
• Subjects: homodimer -- human farnesyltransferase -- interaction; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12862
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Farnesylation is an important post‐translational protein modification in eukaryotes. Farnesylation is performed by protein farnesyltransferase, a heterodimer composed of an α‐ (FTα) and a β‐subunit. Recently, homodimerization of truncated rat and yeast FTα has been detected, suggesting a new role for FTα homodimers in signal transduction. We investigated the putative dimerization behaviour of human and rat FTα. 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. Abstract :