Difference between revisions of "Phosphatase Subfamily PRL"
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PRL is short for Phosphatases of Regenerating Liver. There are three PRLs in human, PRL1, PRL2, PRL3, all of which have been identified as key contributors to metastasis in several human cancers <cite>tremblay14, Von-Hoff06</cite>. The molecular mechanisms of PRL phosphatases is reviewed at here <cite>kohn12</cite> in 2012. | PRL is short for Phosphatases of Regenerating Liver. There are three PRLs in human, PRL1, PRL2, PRL3, all of which have been identified as key contributors to metastasis in several human cancers <cite>tremblay14, Von-Hoff06</cite>. The molecular mechanisms of PRL phosphatases is reviewed at here <cite>kohn12</cite> in 2012. | ||
| − | PRL3 is implicated in cancer. For instance, deletion of PRL3 reduces clonogenicity and tumor-initiation ability of colitis-associated cancer cells in mice <cite>Cramer15</cite>. PRL3 (PTP4A3) independently predicts metastasis and survival in upper tract urothelial carcinoma treated with radical nephroureterectomy <cite></cite>. | + | PRL3 is implicated in cancer. For instance, deletion of PRL3 reduces clonogenicity and tumor-initiation ability of colitis-associated cancer cells in mice <cite>Cramer15</cite>. PRL3 (PTP4A3) independently predicts metastasis and survival in upper tract urothelial carcinoma treated with radical nephroureterectomy <cite>Yeh15</cite>. |
=== References === | === References === | ||
Revision as of 18:26, 15 June 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily PRL (PTP4A)
Evolution
PRL subfamily is present in animals, amoeba, and many basal eukaryotes, but is absent from fungi and plants (unpublish data from gOrtholog).
Domain
PRL has a single domain: phosphatase domain.
Function
PRL is short for Phosphatases of Regenerating Liver. There are three PRLs in human, PRL1, PRL2, PRL3, all of which have been identified as key contributors to metastasis in several human cancers [1, 2]. The molecular mechanisms of PRL phosphatases is reviewed at here [3] in 2012.
PRL3 is implicated in cancer. For instance, deletion of PRL3 reduces clonogenicity and tumor-initiation ability of colitis-associated cancer cells in mice [4]. PRL3 (PTP4A3) independently predicts metastasis and survival in upper tract urothelial carcinoma treated with radical nephroureterectomy [5].
References
- Hardy S, Uetani N, Wong N, Kostantin E, Labbé DP, Bégin LR, Mes-Masson A, Miranda-Saavedra D, and Tremblay ML. The protein tyrosine phosphatase PRL-2 interacts with the magnesium transporter CNNM3 to promote oncogenesis. Oncogene. 2015 Feb 19;34(8):986-95. DOI:10.1038/onc.2014.33 |
- Stephens BJ, Han H, Gokhale V, and Von Hoff DD. PRL phosphatases as potential molecular targets in cancer. Mol Cancer Ther. 2005 Nov;4(11):1653-61. DOI:10.1158/1535-7163.MCT-05-0248 |
- Rios P, Li X, and Köhn M. Molecular mechanisms of the PRL phosphatases. FEBS J. 2013 Jan;280(2):505-24. DOI:10.1111/j.1742-4658.2012.08565.x |
- Cramer JM, Zimmerman MW, Thompson T, Homanics GE, Lazo JS, and Lagasse E. Deletion of Ptp4a3 reduces clonogenicity and tumor-initiation ability of colitis-associated cancer cells in mice. Stem Cell Res. 2014 Jul;13(1):164-171. DOI:10.1016/j.scr.2014.05.004 |
- Yeh HC, Li CC, Huang CN, Hour TC, Yeh BW, Li WM, Liang PI, Chang LL, Li CF, and Wu WJ. PTP4A3 Independently Predicts Metastasis and Survival in Upper Tract Urothelial Carcinoma Treated with Radical Nephroureterectomy. J Urol. 2015 Nov;194(5):1449-55. DOI:10.1016/j.juro.2015.05.101 |
