PTP4A3 explained

Protein tyrosine phosphatase type IVA 3 is an enzyme that in humans is encoded by the PTP4A3 gene.^[1]

The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. Studies of this class of PTPs in mice demonstrated that they were prenylated proteins in vivo, which suggested their association with cell plasma membrane. Overexpression of this gene in mammalian cells was reported to inhibit angiotensin-II induced cell calcium mobilization and promote cell growth. Two alternatively spliced variants exist.

Further reading

• Zeng Q, Hong W, Tan YH . Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1 . Biochem. Biophys. Res. Commun. . 244 . 2 . 421–7 . 1998 . 9514946 . 10.1006/bbrc.1998.8291 .
• Dayton MA, Knobloch TJ . Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38 . Receptors & Signal Transduction . 7 . 4 . 241–56 . 1998 . 9633825 .
• Zeng Q . Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome . J. Biol. Chem. . 275 . 28 . 21444–52 . 2000 . 10747914 . 10.1074/jbc.M000453200 . vanc. Si X . Horstmann H . 3 . Xu . Y . Hong . W . Pallen . CJ . free.
• Matter WF . Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling . Biochem. Biophys. Res. Commun. . 283 . 5 . 1061–8 . 2001 . 11355880 . 10.1006/bbrc.2001.4881 . vanc. Estridge T . Zhang C . 3 . Belagaje . Rama . Stancato . Louis . Dixon . Jeff . Johnson . Brian . Bloem . Laura . Pickard . Todd .
• Saha S . A phosphatase associated with metastasis of colorectal cancer . Science . 294 . 5545 . 1343–6 . 2001 . 11598267 . 10.1126/science.1065817 . Alberto Bardelli . vanc. Bardelli A . Buckhaults P . 3 . Velculescu . VE . Rago . C . St Croix . B . Romans . KE . Choti . MA . Lengauer . C . 2001Sci...294.1343S . 42104960 .
• Wang J, Kirby CE, Herbst R . The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis . J. Biol. Chem. . 277 . 48 . 46659–68 . 2003 . 12235145 . 10.1074/jbc.M206407200 . free .
• Strausberg RL . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . vanc. Feingold EA . Grouse LH . 3 . Derge . JG . Klausner . RD . Collins . FS . Wagner . L . Shenmen . CM . Schuler . GD . 2002PNAS...9916899M . free .
• Pathak MK . Pentamidine is an inhibitor of PRL phosphatases with anticancer activity . Mol. Cancer Ther. . 1 . 14 . 1255–64 . 2003 . 12516958 . vanc. Dhawan D . Lindner DJ . 3 . Borden . EC . Farver . C . Yi . T .
• Zeng Q . PRL-3 and PRL-1 promote cell migration, invasion, and metastasis . Cancer Res. . 63 . 11 . 2716–22 . 2003 . 12782572 . vanc. Dong JM . Guo K . 3 . Li . J . Tan . HX . Koh . V . Pallen . CJ . Manser . E . Hong . W .
• Bardelli A . PRL-3 expression in metastatic cancers . Clin. Cancer Res. . 9 . 15 . 5607–15 . 2004 . 14654542 . vanc. Saha S . Sager JA . 3 . Romans . KE . Xin . B . Markowitz . SD . Lengauer . C . Velculescu . VE . Kinzler . KW .
• Kozlov G . Structural insights into molecular function of the metastasis-associated phosphatase PRL-3 . J. Biol. Chem. . 279 . 12 . 11882–9 . 2004 . 14704153 . 10.1074/jbc.M312905200 . vanc. Cheng J . Ziomek E . 3 . Banville . D . Gehring . K . Ekiel . I . free.
• Kim KA . Structure of human PRL-3, the phosphatase associated with cancer metastasis . FEBS Lett. . 565 . 1–3 . 181–7 . 2004 . 15135076 . 10.1016/j.febslet.2004.03.062 . vanc. Song JS . Jee J . 3 . Sheen . Mee Rie . Lee . Chulhyun . Lee . Tae Gyu . Ro . Seonggu . Cho . Joong Myung . Lee . Weontae . 29552515 . free .
• Wu X . Phosphatase of Regenerating Liver-3 Promotes Motility and Metastasis of Mouse Melanoma Cells . Am. J. Pathol. . 164 . 6 . 2039–54 . 2004 . 15161639 . 10.1016/S0002-9440(10)63763-7. 1615773 . vanc. Zeng H . Zhang X . 3 . Zhao . Y . Sha . H . Ge . X . Zhang . M . Gao . X . Xu . Q .
• Gerhard DS . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . vanc. Wagner L . Feingold EA . 3 . Shenmen . CM . Grouse . LH . Schuler . G . Klein . SL . Old . S . Rasooly . R .
• Kato H . High expression of PRL-3 promotes cancer cell motility and liver metastasis in human colorectal cancer: a predictive molecular marker of metachronous liver and lung metastases . Clin. Cancer Res. . 10 . 21 . 7318–28 . 2005 . 15534108 . 10.1158/1078-0432.CCR-04-0485 . vanc. Semba S . Miskad UA . 3 . Seo . Y . Kasuga . M . Yokozaki . H . free.
• Li J . Generation of PRL-3- and PRL-1-specific monoclonal antibodies as potential diagnostic markers for cancer metastases . Clin. Cancer Res. . 11 . 6 . 2195–204 . 2005 . 15788667 . 10.1158/1078-0432.CCR-04-1984 . vanc. Guo K . Koh VW . 3 . Tang . JP . Gan . BQ . Shi . H . Li . HX . Zeng . Q . free .
• Polato F . PRL-3 phosphatase is implicated in ovarian cancer growth . Clin. Cancer Res. . 11 . 19 Pt 1 . 6835–9 . 2006 . 16203771 . 10.1158/1078-0432.CCR-04-2357 . vanc. Codegoni A . Fruscio R . 3 . Perego . P . Mangioni . C . Saha . S . Bardelli . A . Broggini . M . free .
• Peng L . Identification of integrin alpha1 as an interacting protein of protein tyrosine phosphatase PRL-3 . Biochem. Biophys. Res. Commun. . 342 . 1 . 179–83 . 2006 . 16472776 . 10.1016/j.bbrc.2006.01.102 . vanc. Jin G . Wang L . 3 . Guo . Jianpin . Meng . Lin . Shou . Chengchao .
• Rouleau C . Protein tyrosine phosphatase PRL-3 in malignant cells and endothelial cells: expression and function . Mol. Cancer Ther. . 5 . 2 . 219–29 . 2006 . 16505094 . 10.1158/1535-7163.MCT-05-0289 . vanc. Roy A . St Martin T . 3 . Dufault . MR . Boutin . P . Liu . D . Zhang . M . Puorro-Radzwill . K . Rulli . L . free .
• Radke I . Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer . Br. J. Cancer . 95 . 3 . 347–54 . 2006 . 16832410 . 10.1038/sj.bjc.6603261 . 2360632 . vanc. Götte M . Kersting C . 3 . Mattsson . B . Kiesel . L . Wülfing . P .

Notes and References

1. Web site: Entrez Gene: PTP4A3 protein tyrosine phosphatase type IVA, member 3.