biostudies-literatureUnknown13(9B)Pascaru MIn order to analyse whether a C-terminal polybasic sequence represents a nuclear localization signal (NLS) we obtained several truncated and mutant forms of protein of regerating liver (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 analysed 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 transJournal of cellular and molecular medicine3141-50https://www.ebi.ac.uk/biostudies/studies/S-EPMC4516473biostudies-literatureAnalysis of molecular determinants of PRL-3.PMC4516473Popescu ITanase CBoeti PSzedlacsek SEVacaru AMNeagu EPascaru MfalseAnalysis of molecular determinants of PRL-3.In order to analyse whether a C-terminal polybasic sequence represents a nuclear localization signal (NLS) we obtained several truncated and mutant forms of protein of regerating liver (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 analysed 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 trans2009-01-01T00:00:00Z2009 Sep2025-04-27T02:51:34.458Z2019-03-26T23:36:54ZS-EPMC45164731904041910.1111/j.1582-4934.2008.00591.x