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PPP2R4

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

{{Infobox_gene}}

Serine/threonine-protein phosphatase 2A regulatory subunit B is an enzyme that in humans is encoded by the PPP2R4 gene.{{cite journal |vauthors=Van Hoof C, Aly MS, Garcia A, Cayla X, Cassiman JJ, Merlevede W, Goris J | title = Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A | journal = Genomics | volume = 28 | issue = 2 | pages = 261–72 |date=Feb 1996 | pmid = 8530035 | doi = 10.1006/geno.1995.1140 }}{{cite web | title = Entrez Gene: PPP2R4 protein phosphatase 2A activator, regulatory subunit 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5524}}

Protein phosphatase 2A is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2A holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B' family. This gene encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A. Alternative splicing results in multiple transcript variants encoding different isoforms.

Interactions

PPP2R4 has been shown to interact with PPP2R3A,{{cite journal |last=Davis |first=Anthony J |author2=Yan Zhen |author3=Martinez Bobbie |author4=Mumby Marc C |date=Jun 2008 |title=Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit |journal=J. Biol. Chem. |volume=283 |issue=23 |pages=16104–14 |location = United States| issn = 0021-9258| pmid = 18397887 |doi = 10.1074/jbc.M710313200 |pmc=2414307 |doi-access=free }} CCNG1{{cite journal |last=Okamoto |first=K |author2=Kamibayashi C |author3=Serrano M |author4=Prives C |author5=Mumby M C |author6=Beach D |date=Nov 1996 |title=p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A |journal=Mol. Cell. Biol. |volume=16 |issue=11 |pages=6593–602 |location = UNITED STATES| issn = 0270-7306| pmid = 8887688 |pmc=231661 |doi=10.1128/mcb.16.11.6593 }} and Janus kinase 2.{{cite journal |doi=10.1006/bbrc.1996.1023 |last=Fuhrer |first=D K |author2=Yang Y C |date=Jul 1996 |title=Complex formation of JAK2 with PP2A, P13K, and Yes in response to the hematopoietic cytokine interleukin-11 |journal=Biochem. Biophys. Res. Commun. |volume=224 |issue=2 |pages=289–96 |location = UNITED STATES| issn = 0006-291X| pmid = 8702385 }}

References

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Further reading

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  • {{cite journal |vauthors=Andersen JL, Planelles V |title=The role of Vpr in HIV-1 pathogenesis. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 43–51 |year= 2005 |pmid= 15638722 |doi=10.2174/1570162052772988 }}
  • {{cite journal |vauthors=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 | pmc=554975 |doi-access=free }}
  • {{cite journal |vauthors=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143–9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279 |doi-access= free }}
  • {{cite journal |vauthors=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270–86 |year= 2005 |pmid= 15817944 }}
  • {{cite journal |vauthors=Soprano KJ, Purev E, Vuocolo S, Soprano DR |title=Rb2/p130 and protein phosphatase 2A: key mediators of ovarian carcinoma cell growth suppression by all-trans retinoic acid. |journal=Oncogene |volume=25 |issue= 38 |pages= 5315–25 |year= 2006 |pmid= 16936753 |doi= 10.1038/sj.onc.1209679 |doi-access= free }}
  • {{cite journal |vauthors=Jakes S, Mellgren RL, Schlender KK |title=Isolation and characterization of an inhibitor-sensitive and a polycation-stimulated protein phosphatase from rat liver nuclei. |journal=Biochim. Biophys. Acta |volume=888 |issue= 1 |pages= 135–42 |year= 1986 |pmid= 3017441 |doi=10.1016/0167-4889(86)90079-0 }}
  • {{cite journal |vauthors=Turowski P, Fernandez A, Favre B, etal |title=Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. |journal=J. Cell Biol. |volume=129 |issue= 2 |pages= 397–410 |year= 1995 |pmid= 7721943 |doi=10.1083/jcb.129.2.397 | pmc=2199911 }}
  • {{cite journal |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
  • {{cite journal |vauthors=Cayla X, Van Hoof C, Bosch M, etal |title=Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A. |journal=J. Biol. Chem. |volume=269 |issue= 22 |pages= 15668–75 |year= 1994 |doi=10.1016/S0021-9258(17)40733-2 |pmid= 8195217 |doi-access=free }}
  • {{cite journal |vauthors=Okamoto K, Kamibayashi C, Serrano M, etal |title=p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6593–602 |year= 1996 |pmid= 8887688 |doi= 10.1128/mcb.16.11.6593| pmc=231661 }}
  • {{cite journal |vauthors=Tung HY, De Rocquigny H, Zhao LJ, etal |title=Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr. |journal=FEBS Lett. |volume=401 |issue= 2–3 |pages= 197–201 |year= 1997 |pmid= 9013886 |doi=10.1016/S0014-5793(96)01470-6 |s2cid=23293768 |doi-access=free }}
  • {{cite journal |vauthors=Hériché JK, Lebrin F, Rabilloud T, etal |title=Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha. |journal=Science |volume=276 |issue= 5314 |pages= 952–5 |year= 1997 |pmid= 9139659 |doi=10.1126/science.276.5314.952 }}
  • {{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal |vauthors=Ruediger R, Brewis N, Ohst K, Walter G |title=Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production. |journal=Virology |volume=238 |issue= 2 |pages= 432–43 |year= 1998 |pmid= 9400615 |doi= 10.1006/viro.1997.8873 |doi-access= free }}
  • {{cite journal |vauthors=Ogris E, Du X, Nelson KC, etal |title=A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 14382–91 |year= 1999 |pmid= 10318862 |doi=10.1074/jbc.274.20.14382 |pmc=3503312|doi-access=free }}
  • {{cite journal |vauthors=Janssens V, Van Hoof C, De Baere I, etal |title=Functional analysis of the promoter region of the human phosphotyrosine phosphatase activator gene: Yin Yang 1 is essential for core promoter activity. |journal=Biochem. J. |volume=344 |issue= 3|pages= 755–63 |year= 2000 |pmid= 10585862 |doi= 10.1042/0264-6021:3440755| pmc=1220697 }}
  • {{cite journal |vauthors=Janssens V, van Hoof C, Martens E, etal |title=Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene. |journal=Eur. J. Biochem. |volume=267 |issue= 14 |pages= 4406–13 |year= 2000 |pmid= 10880964 |doi=10.1046/j.1432-1327.2000.01486.x |doi-access=free }}
  • {{cite journal |vauthors=Elder RT, Yu M, Chen M, etal |title=HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25. |journal=Virology |volume=287 |issue= 2 |pages= 359–70 |year= 2001 |pmid= 11531413 |doi= 10.1006/viro.2001.1007 |doi-access= free }}

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