| 释义 |
- Interactions
- References
- Further reading
{{Infobox_gene}}Serine/threonine-protein phosphatase 2A regulatory subunit B' is an enzyme that in humans is encoded by the PPP2R4 gene.[1][2]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.[2] InteractionsPPP2R4 has been shown to interact with PPP2R3A,[3] CCNG1[4] and Janus kinase 2.[5] References1. ^{{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 | pmc = | doi = 10.1006/geno.1995.1140 }}
2. ^1 {{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| accessdate = }}
3. ^{{cite journal |last=Davis |first=Anthony J |authorlink= |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 |publisher= |location = United States| issn = 0021-9258| pmid = 18397887 |doi = 10.1074/jbc.M710313200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=2414307 }}
4. ^{{cite journal |last=Okamoto |first=K |authorlink= |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 |publisher= |location = UNITED STATES| issn = 0270-7306| pmid = 8887688 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=231661 }}
5. ^{{cite journal |doi=10.1006/bbrc.1996.1023 |last=Fuhrer |first=D K |authorlink= |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 |publisher= |location = UNITED STATES| issn = 0006-291X| pmid = 8702385 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
Further reading{{refbegin | 2}}- {{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 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 | pmc=554975 }}
- {{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 }}
- {{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 |doi= }}
- {{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 }}
- {{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 |pmid= 8195217 |doi= }}
- {{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= | 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 }}
- {{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 }}
- {{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}}
- {{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 }}
- {{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 }}
{{refend}}{{PDB Gallery|geneid=5524}}{{Gene-9-stub}} |