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Type: Journal article
Title: Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation
Author: Wadham, C.
Gamble, J.
Vadas, M.
Khew-Goodall, Y.
Citation: Journal of Cell Science, 2000; 113(17):3117-3123
Publisher: Company of Biologists Ltd
Issue Date: 2000
ISSN: 0021-9533
Statement of
Carol Wadham, Jennifer R. Gamble, Mathew A. Vadas and Yeesim Khew-Goodall
Abstract: Pez is a non-transmembrane tyrosine phosphatase with homology to the FERM (4.1, ezrin, radixin, moesin) family of proteins. The subcellular localisation of Pez in endothelial cells was found to be regulated by cell density and serum concentration. In confluent monolayers Pez was cytoplasmic, but in cells cultured at low density Pez was nuclear, suggesting that it is a nuclear protein in proliferating cells. This notion is supported by the loss of nuclear Pez when cells are serum-starved to induce quiescence, and the rapid return of Pez to the nucleus upon refeeding with serum to induce proliferation. Vascular endothelial cells normally exist as a quiescent confluent monolayer but become proliferative during angiogenesis or upon vascular injury. Using a 'wound' assay to mimic these events in vitro, Pez was found to be nuclear in the cells that had migrated and were proliferative at the 'wound' edge. TGFbeta, which inhibits cell proliferation but not migration, inhibited the translocation of Pez to the nucleus in the cells at the 'wound' edge, further strengthening the argument that Pez plays a role in the nucleus during cell proliferation. Together, the data presented indicate that Pez is a nuclear tyrosine phosphatase that may play a role in cell proliferation.
Keywords: Tyrosine phosphatase; Pez; Nuclear localisation; HUVEC; Proliferation; Quiescence
Rights: ┬ęThe Company of Biologists Limited 2000
RMID: 0001001246
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