Biology:PPP2R4
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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]
Interactions
PPP2R4 has been shown to interact with PPP2R3A,[3] CCNG1[4] and Janus kinase 2.[5]
References
- ↑ "Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A". Genomics 28 (2): 261–72. Feb 1996. doi:10.1006/geno.1995.1140. PMID 8530035.
- ↑ 2.0 2.1 "Entrez Gene: PPP2R4 protein phosphatase 2A activator, regulatory subunit 4". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5524.
- ↑ Davis, Anthony J; Yan Zhen; Martinez Bobbie; Mumby Marc C (Jun 2008). "Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit". J. Biol. Chem. (United States) 283 (23): 16104–14. doi:10.1074/jbc.M710313200. ISSN 0021-9258. PMID 18397887.
- ↑ Okamoto, K; Kamibayashi C; Serrano M; Prives C; Mumby M C; Beach D (Nov 1996). "p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A". Mol. Cell. Biol. (UNITED STATES) 16 (11): 6593–602. doi:10.1128/mcb.16.11.6593. ISSN 0270-7306. PMID 8887688.
- ↑ Fuhrer, D K; Yang Y C (Jul 1996). "Complex formation of JAK2 with PP2A, P13K, and Yes in response to the hematopoietic cytokine interleukin-11". Biochem. Biophys. Res. Commun. (UNITED STATES) 224 (2): 289–96. doi:10.1006/bbrc.1996.1023. ISSN 0006-291X. PMID 8702385.
Further reading
- "The role of Vpr in HIV-1 pathogenesis.". Curr. HIV Res. 3 (1): 43–51. 2005. doi:10.2174/1570162052772988. PMID 15638722.
- "The Vpr protein from HIV-1: distinct roles along the viral life cycle.". Retrovirology 2: 11. 2006. doi:10.1186/1742-4690-2-11. PMID 15725353.
- "Viral infections and cell cycle G2/M regulation.". Cell Res. 15 (3): 143–9. 2005. doi:10.1038/sj.cr.7290279. PMID 15780175.
- "HIV-1 viral protein R (Vpr) & host cellular responses.". Indian J. Med. Res. 121 (4): 270–86. 2005. PMID 15817944.
- "Rb2/p130 and protein phosphatase 2A: key mediators of ovarian carcinoma cell growth suppression by all-trans retinoic acid.". Oncogene 25 (38): 5315–25. 2006. doi:10.1038/sj.onc.1209679. PMID 16936753.
- "Isolation and characterization of an inhibitor-sensitive and a polycation-stimulated protein phosphatase from rat liver nuclei.". Biochim. Biophys. Acta 888 (1): 135–42. 1986. doi:10.1016/0167-4889(86)90079-0. PMID 3017441.
- "Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression.". J. Cell Biol. 129 (2): 397–410. 1995. doi:10.1083/jcb.129.2.397. PMID 7721943.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A.". J. Biol. Chem. 269 (22): 15668–75. 1994. doi:10.1016/S0021-9258(17)40733-2. PMID 8195217.
- "p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A.". Mol. Cell. Biol. 16 (11): 6593–602. 1996. doi:10.1128/mcb.16.11.6593. PMID 8887688.
- "Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr.". FEBS Lett. 401 (2–3): 197–201. 1997. doi:10.1016/S0014-5793(96)01470-6. PMID 9013886.
- "Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha.". Science 276 (5314): 952–5. 1997. doi:10.1126/science.276.5314.952. PMID 9139659.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production.". Virology 238 (2): 432–43. 1998. doi:10.1006/viro.1997.8873. PMID 9400615.
- "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A.". J. Biol. Chem. 274 (20): 14382–91. 1999. doi:10.1074/jbc.274.20.14382. PMID 10318862.
- "Functional analysis of the promoter region of the human phosphotyrosine phosphatase activator gene: Yin Yang 1 is essential for core promoter activity.". Biochem. J. 344 (3): 755–63. 2000. doi:10.1042/0264-6021:3440755. PMID 10585862.
- "Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene.". Eur. J. Biochem. 267 (14): 4406–13. 2000. doi:10.1046/j.1432-1327.2000.01486.x. PMID 10880964.
- "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.". Virology 287 (2): 359–70. 2001. doi:10.1006/viro.2001.1007. PMID 11531413.
PDB gallery | |
|---|---|
|
 |  |
