PTP4A1 explained
Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene.[1]
The protein encoded by this gene belongs to a small class of prenylated protein tyrosine phosphatases (PTPs), which contains a PTP domain and a characteristic C-terminal prenylation motif. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This tyrosine phosphatase is a nuclear protein, but may primarily associate with plasma membrane. The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which implicated its role in the tumorigenesis. Studies in rat suggested that this gene may be an immediate-early gene in mitogen-stimulated cells.[2]
Interactions
PTP4A1 has been shown to interact with ATF7.[3]
Further reading
- Cates CA, Michael RL, Stayrook KR, etal . Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases . Cancer Lett. . 110 . 1–2 . 49–55 . 1997 . 9018080 . 10.1016/S0304-3835(96)04459-X .
- 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 .
- Tsujimoto H, Nishizuka S, Redpath JL, Stanbridge EJ . Differential gene expression in tumorigenic and nontumorigenic HeLa x normal human fibroblast hybrid cells . Mol. Carcinog. . 26 . 4 . 298–304 . 1999 . 10569806 . 10.1002/(SICI)1098-2744(199912)26:4<298::AID-MC8>3.0.CO;2-M . 21209686 .
- Zeng Q, Si X, Horstmann H, etal . 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 . free .
- Gjörloff-Wingren A, Saxena M, Han S, etal . Subcellular localization of intracellular protein tyrosine phosphatases in T cells . Eur. J. Immunol. . 30 . 8 . 2412–21 . 2000 . 10940933 . 10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J . 8132613 .
- Peters CS, Liang X, Li S, etal . ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase . J. Biol. Chem. . 276 . 17 . 13718–26 . 2001 . 11278933 . 10.1074/jbc.M011562200 . free .
- Si X, Zeng Q, Ng CH, etal . Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II . J. Biol. Chem. . 276 . 35 . 32875–82 . 2001 . 11447212 . 10.1074/jbc.M010400200 . free .
- Nicolas G, Fournier CM, Galand C, etal . Tyrosine Phosphorylation Regulates Alpha II Spectrin Cleavage by Calpain . Mol. Cell. Biol. . 22 . 10 . 3527–36 . 2002 . 11971983 . 10.1128/MCB.22.10.3527-3536.2002 . 133798 .
- 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, Feingold EA, Grouse LH, etal . 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 . 2002PNAS...9916899M . free .
- Pathak MK, Dhawan D, Lindner DJ, etal . Pentamidine is an inhibitor of PRL phosphatases with anticancer activity . Mol. Cancer Ther. . 1 . 14 . 1255–64 . 2003 . 12516958 .
- Zeng Q, Dong JM, Guo K, etal . PRL-3 and PRL-1 promote cell migration, invasion, and metastasis . Cancer Res. . 63 . 11 . 2716–22 . 2003 . 12782572 .
- Mungall AJ, Palmer SA, Sims SK, etal . The DNA sequence and analysis of human chromosome 6 . Nature . 425 . 6960 . 805–11 . 2003 . 14574404 . 10.1038/nature02055 . free . 2003Natur.425..805M .
- Werner SR, Lee PA, DeCamp MW, etal . Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases . Cancer Lett. . 202 . 2 . 201–11 . 2004 . 14643450 . 10.1016/S0304-3835(03)00517-2 .
- Gerhard DS, Wagner L, Feingold EA, etal . 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 .
- Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P . Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach . Toxicon . 44 . 6 . 597–608 . 2005 . 15501285 . 10.1016/j.toxicon.2004.07.018 .
- Jeong DG, Kim SJ, Kim JH, etal . Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms . J. Mol. Biol. . 345 . 2 . 401–13 . 2005 . 15571731 . 10.1016/j.jmb.2004.10.061 .
- Sun JP, Wang WQ, Yang H, etal . Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion . Biochemistry . 44 . 36 . 12009–21 . 2005 . 16142898 . 10.1021/bi0509191 .
- Radke I, Götte M, Kersting C, etal . 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 .
Notes and References
- Peng Y, Genin A, Spinner NB, Diamond RH, Taub R . The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer . J Biol Chem . 273 . 27 . 17286–95 . Aug 1998 . 9642300 . 10.1074/jbc.273.27.17286 . free .
- Web site: Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1.
- Peters . C S . Liang X . Li S . Kannan S . Peng Y . Taub R . Diamond R H . Apr 2001 . ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase . J. Biol. Chem. . 276 . 17 . 13718–26 . United States. 0021-9258. 11278933 . 10.1074/jbc.M011562200 . free .