Difference between revisions of "Phosphatase Subfamily PRL"

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=== Domain ===
 
=== Domain ===
 
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PRL has a single domain: phosphatase domain.
  
 
=== Function ===  
 
=== Function ===  

Revision as of 05:09, 27 February 2015

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 (e.g. [1]).

References

  1. 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 | PubMed ID:24632616 | HubMed [tremblay14]
  2. 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 | PubMed ID:16275986 | HubMed [Von-Hoff06]
  3. 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 | PubMed ID:22413991 | HubMed [kohn12]
All Medline abstracts: PubMed | HubMed