Phosphatase Subfamily PRL
From PhosphataseWiki
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily PRL
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, but it may play other roles as more works are going-on. For example. deletion of PRL3 reduces clonogenicity and tumor-initiation ability of colitis-associated cancer cells in mice [4].
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 |
