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Exploring the putative self‐binding property of the human farnesyltransferase alpha‐subunit
Author(s) -
Hagemann Anna,
Müller Grit,
Manthey Iris,
Bachmann Hagen S.
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12862
Subject(s) - farnesyltransferase , prenylation , farnesyltransferase inhibitor , protein subunit , in vitro , biochemistry , yeast , in vivo , microbiology and biotechnology , signal transduction , chemistry , enzyme , biology , gene , genetics
Farnesylation is an important post‐translational protein modification in eukaryotes. Farnesylation is performed by protein farnesyltransferase, a heterodimer composed of an α‐ ( FT α) and a β‐subunit. Recently, homodimerization of truncated rat and yeast FT α has been detected, suggesting a new role for FT α homodimers in signal transduction. We investigated the putative dimerization behaviour of human and rat FT α. 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 FT ase in different species and may be important for the ongoing development of FT ase inhibitors.