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PTP4A1

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene.{{cite journal |vauthors=Peng Y, Genin A, Spinner NB, Diamond RH, Taub R | title = The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer | journal = J Biol Chem | volume = 273 | issue = 27 | pages = 17286–95 |date=Aug 1998 | pmid = 9642300 | doi =10.1074/jbc.273.27.17286 | doi-access = free }}

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.{{cite web | title = Entrez Gene: PTP4A1 protein tyrosine phosphatase type IVA, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7803}}

Interactions

PTP4A1 has been shown to interact with ATF7.{{cite journal |last=Peters |first=C S |author2=Liang X |author3=Li S |author4=Kannan S |author5=Peng Y |author6=Taub R |author7=Diamond R H |date=Apr 2001 |title=ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase |journal=J. Biol. Chem. |volume=276 |issue=17 |pages=13718–26 |location = United States| issn = 0021-9258| pmid = 11278933 |doi = 10.1074/jbc.M011562200 |doi-access=free }}

References

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Further reading

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  • {{cite journal |vauthors=Cates CA, Michael RL, Stayrook KR, etal |title=Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases |journal=Cancer Lett. |volume=110 |issue= 1–2 |pages= 49–55 |year= 1997 |pmid= 9018080 |doi=10.1016/S0304-3835(96)04459-X }}
  • {{cite journal |vauthors=Dayton MA, Knobloch TJ |title=Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38 |journal=Receptors & Signal Transduction |volume=7 |issue= 4 |pages= 241–56 |year= 1998 |pmid= 9633825 }}
  • {{cite journal |vauthors=Tsujimoto H, Nishizuka S, Redpath JL, Stanbridge EJ |title=Differential gene expression in tumorigenic and nontumorigenic HeLa x normal human fibroblast hybrid cells |journal=Mol. Carcinog. |volume=26 |issue= 4 |pages= 298–304 |year= 1999 |pmid= 10569806 |doi=10.1002/(SICI)1098-2744(199912)26:4<298::AID-MC8>3.0.CO;2-M |s2cid=21209686 }}
  • {{cite journal |vauthors=Zeng Q, Si X, Horstmann H, etal |title=Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21444–52 |year= 2000 |pmid= 10747914 |doi= 10.1074/jbc.M000453200 |doi-access= free }}
  • {{cite journal |vauthors=Gjörloff-Wingren A, Saxena M, Han S, etal |title=Subcellular localization of intracellular protein tyrosine phosphatases in T cells |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2412–21 |year= 2000 |pmid= 10940933 |doi=10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J |s2cid=8132613 }}
  • {{cite journal |vauthors=Peters CS, Liang X, Li S, etal |title=ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 13718–26 |year= 2001 |pmid= 11278933 |doi= 10.1074/jbc.M011562200 |doi-access= free }}
  • {{cite journal |vauthors=Si X, Zeng Q, Ng CH, etal |title=Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase II |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32875–82 |year= 2001 |pmid= 11447212 |doi= 10.1074/jbc.M010400200 |doi-access= free }}
  • {{cite journal |vauthors=Nicolas G, Fournier CM, Galand C, etal |title=Tyrosine Phosphorylation Regulates Alpha II Spectrin Cleavage by Calpain |journal=Mol. Cell. Biol. |volume=22 |issue= 10 |pages= 3527–36 |year= 2002 |pmid= 11971983 |doi=10.1128/MCB.22.10.3527-3536.2002 | pmc=133798 }}
  • {{cite journal |vauthors=Wang J, Kirby CE, Herbst R |title=The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 46659–68 |year= 2003 |pmid= 12235145 |doi= 10.1074/jbc.M206407200 |doi-access= free }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Pathak MK, Dhawan D, Lindner DJ, etal |title=Pentamidine is an inhibitor of PRL phosphatases with anticancer activity |journal=Mol. Cancer Ther. |volume=1 |issue= 14 |pages= 1255–64 |year= 2003 |pmid= 12516958 }}
  • {{cite journal |vauthors=Zeng Q, Dong JM, Guo K, etal |title=PRL-3 and PRL-1 promote cell migration, invasion, and metastasis |journal=Cancer Res. |volume=63 |issue= 11 |pages= 2716–22 |year= 2003 |pmid= 12782572 }}
  • {{cite journal |vauthors=Mungall AJ, Palmer SA, Sims SK, etal |title=The DNA sequence and analysis of human chromosome 6 |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 |doi-access= free |bibcode= 2003Natur.425..805M }}
  • {{cite journal |vauthors=Werner SR, Lee PA, DeCamp MW, etal |title=Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases |journal=Cancer Lett. |volume=202 |issue= 2 |pages= 201–11 |year= 2004 |pmid= 14643450 |doi=10.1016/S0304-3835(03)00517-2 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Raghavendra Prasad HS, Qi Z, Srinivasan KN, Gopalakrishnakone P |title=Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach |journal=Toxicon |volume=44 |issue= 6 |pages= 597–608 |year= 2005 |pmid= 15501285 |doi= 10.1016/j.toxicon.2004.07.018 }}
  • {{cite journal |vauthors=Jeong DG, Kim SJ, Kim JH, etal |title=Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms |journal=J. Mol. Biol. |volume=345 |issue= 2 |pages= 401–13 |year= 2005 |pmid= 15571731 |doi= 10.1016/j.jmb.2004.10.061 }}
  • {{cite journal |vauthors=Sun JP, Wang WQ, Yang H, etal |title=Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion |journal=Biochemistry |volume=44 |issue= 36 |pages= 12009–21 |year= 2005 |pmid= 16142898 |doi= 10.1021/bi0509191 }}
  • {{cite journal |vauthors=Radke I, Götte M, Kersting C, etal |title=Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer |journal=Br. J. Cancer |volume=95 |issue= 3 |pages= 347–54 |year= 2006 |pmid= 16832410 |doi= 10.1038/sj.bjc.6603261 | pmc=2360632 }}

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