Analysis of molecular determinants of PRL-3

J Cell Mol Med. 2009 Sep;13(9B):3141-50. doi: 10.1111/j.1582-4934.2008.00591.x. Epub 2008 Jun 28.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • CHO Cells
  • COS Cells
  • Chlorocebus aethiops
  • Cricetinae
  • Cricetulus
  • Gene Expression Regulation*
  • HeLa Cells
  • Humans
  • Kinetics
  • Liver / pathology
  • Mutation
  • Neoplasm Proteins / genetics*
  • Neoplasm Proteins / metabolism
  • Phosphoric Monoester Hydrolases / metabolism
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatases / genetics*
  • Protein Tyrosine Phosphatases / metabolism
  • Regeneration

Substances

  • Neoplasm Proteins
  • Phosphoric Monoester Hydrolases
  • PTP4A3 protein, human
  • Protein Tyrosine Phosphatases