Scopul nostru este sprijinirea şi promovarea cercetării ştiinţifice şi facilitarea comunicării între cercetătorii români din întreaga lume.
Autori: Pascaru M, Tanase C, Vacaru AM, Boeti P, Neagu E, Popescu I, Szedlacsek SE.
Editorial: J Cell Mol Med, 13(9B), p.3141-50, 2008.
In order to analyze whether a C-terminal polybasic sequence represents a nuclear localization signal (NLS) we obtained several truncated and mutant forms of PRL-3 and evaluated their subcellular localization as compared to the wild type form. Our results invalidate the hypothesis that this is an NLS. We also analyzed the influence of the C- and N-terminal residues on the phosphatase activity of PRL-3. Our results provide in vitro evidence that the C-terminal CAAX motif, besides directing the protein farnesylation, plays an additional regulatory role by inhibiting the catalytic efficiency of PRL-3. Taking into account the results we obtained as well as reported data we propose a hypothetical molecular mechanism for the nucleocytoplasmic localization and transfer of PRL-3.
Cuvinte cheie: PRL-3 • subcellular localization • oligomerization • catalytic activity • steady-state parameters