Difference between revisions of "Phosphatase Subfamily PRL"
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| − | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_PRL|Subfamily PRL]] | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_PRL|Subfamily PRL]] (PTP4A) |
| − | PRL | + | === Evolution === |
| + | PRL is present in animals, and most basal eukaryotes, but is absent from fungi and plants ([http://resdev.gene.com/gOrtholog/view/cluster/MC0001030/overview unpublished data from gOrtholog]). | ||
| − | ===== | + | === Domain === |
| + | PRL has a [[Phosphatase_Fold_CC1|CC1]] fold phosphatase domain followed by a polybasic motif and a consensus prenylation motif. | ||
| + | |||
| + | === Function === | ||
| + | PRL is short for Phosphatases of Regenerating Liver. There are three PRLs in human, PRL1, PRL2, PRL3 (PTP4A1-3), 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 has been reviewed <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>Yeh15</cite>. | ||
| + | |||
| + | PTP4A3 has a number of reported protein substrates including ezrin <cite>Forte</cite> and p130cas <cite>Matter</cite>. All three human genes have activity against tyrosine-phosphorylated peptides <cite>Pathak</cite>. | ||
| + | |||
| + | === References === | ||
<biblio> | <biblio> | ||
| + | #Cramer15 pmid=24950307 | ||
#Von-Hoff06 pmid=16275986 | #Von-Hoff06 pmid=16275986 | ||
#tremblay14 pmid=24632616 | #tremblay14 pmid=24632616 | ||
| + | #Forte pmid=18078820 | ||
#kohn12 pmid=22413991 | #kohn12 pmid=22413991 | ||
| + | #Matter pmid=11355880 | ||
| + | #Pathak pmid=12516958 | ||
| + | #Yeh15 pmid=26070892 | ||
</biblio> | </biblio> | ||
Latest revision as of 08:01, 26 July 2017
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily PRL (PTP4A)
Evolution
PRL is present in animals, and most basal eukaryotes, but is absent from fungi and plants (unpublished data from gOrtholog).
Domain
PRL has a CC1 fold phosphatase domain followed by a polybasic motif and a consensus prenylation motif.
Function
PRL is short for Phosphatases of Regenerating Liver. There are three PRLs in human, PRL1, PRL2, PRL3 (PTP4A1-3), all of which have been identified as key contributors to metastasis in several human cancers [1, 2]. The molecular mechanisms of PRL phosphatases has been reviewed [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].
PTP4A3 has a number of reported protein substrates including ezrin [6] and p130cas [7]. All three human genes have activity against tyrosine-phosphorylated peptides [8].
References
Error fetching PMID 16275986:
Error fetching PMID 24632616:
Error fetching PMID 18078820:
Error fetching PMID 22413991:
Error fetching PMID 11355880:
Error fetching PMID 12516958:
Error fetching PMID 26070892:
- Error fetching PMID 24632616:
- Error fetching PMID 16275986:
- Error fetching PMID 22413991:
- Error fetching PMID 24950307:
- Error fetching PMID 26070892:
- Error fetching PMID 18078820:
- Error fetching PMID 11355880:
- Error fetching PMID 12516958:
