Open AccessAnalysis of molecular determinants of PRL‐3
Author(s) -
Pascaru Mihaela,
Tanase Carmen,
Vacaru Andrei M.,
Boeti Patricia,
Neagu Elena,
Popescu Irinel,
Szedlacsek Stefan E.
Publication year - 2009
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/j.1582-4934.2008.00591.x
Subject(s) - nls , nuclear localization sequence , subcellular localization , prenylation , mutant , phosphatase , nuclear transport , microbiology and biotechnology , cytosol , in vitro , biology , chemistry , biochemistry , phosphorylation , computational biology , enzyme , cell nucleus , gene , cytoplasm
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 transfer of PRL‐3.