Volume 13, Issue 9b pp. 3141-3150

Analysis of molecular determinants of PRL-3

Mihaela Pascaru

Mihaela Pascaru

Department of Enzymology, Institute of Biochemistry, Bucharest, Romania

These authors contributed equally to this work.

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Carmen Tanase

Carmen Tanase

Department of Enzymology, Institute of Biochemistry, Bucharest, Romania

These authors contributed equally to this work.

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Andrei M. Vacaru

Andrei M. Vacaru

Department of Enzymology, Institute of Biochemistry, Bucharest, Romania

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Patricia Boeti

Patricia Boeti

Center of General Surgery and Liver Transplantation, Fundeni Clinical Institute, Bucharest

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Elena Neagu

Elena Neagu

Center of Bioanalysis, National Institute for Research – Development of Biological Sciences, Bucharest, Romania

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Irinel Popescu

Irinel Popescu

Center of General Surgery and Liver Transplantation, Fundeni Clinical Institute, Bucharest

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Stefan E. Szedlacsek

Corresponding Author

Stefan E. Szedlacsek

Department of Enzymology, Institute of Biochemistry, Bucharest, Romania

Correspondence to: Stefan E. SZEDLACSEK, Department of Enzymology / Institute of Biochemistry, Spl. Independentei 296, 060031 Bucharest, Romania.
Tel.: + 40-21-2239069
Fax: +40-21-2239068
E-mail: [email protected]Search for more papers by this author
First published: 29 January 2010
Citations: 16

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.

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