PPP2R2A

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform is an enzyme regulator that in humans is encoded by the PPP2R2A gene.[5]

PPP2R2A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3DW8
Identifiers
Aliases	PPP2R2A, B55A, B55ALPHA, PR52A, PR55A, protein phosphatase 2 regulatory subunit Balpha, PR55alpha
External IDs	OMIM: 604941 MGI: 1919228 HomoloGene: 2035 GeneCards: PPP2R2A
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p21.2 Start 26,291,508 bp[1] End 26,372,680 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 D1 Start 67,014,056 bp[2] End 67,072,444 bp[2]
Gene ontology Molecular function • GO:0001948 protein binding • protein serine/threonine phosphatase activity • protein phosphatase regulator activity • GO:0032403 macromolecular complex binding • tau protein binding • protein phosphatase 2A binding Cellular component • nucleoplasm • protein phosphatase type 2A complex • cytosol • synapse • glutamatergic synapse Biological process • response to morphine • G2/M transition of mitotic cell cycle • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • protein dephosphorylation • GO:0007067 mitotic cell cycle • peptidyl-serine dephosphorylation • developmental process • regulation of phosphoprotein phosphatase activity • mitotic nuclear envelope reassembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5520	71978
Ensembl	ENSG00000221914	ENSMUSG00000022052
UniProt	P63151	Q6P1F6
RefSeq (mRNA)	NM_001177591 NM_002717	NM_001205188 NM_028032 NM_001360033 NM_001360034
RefSeq (protein)	NP_001171062 NP_002708	NP_001192117 NP_082308 NP_001346962 NP_001346963
Location (UCSC)	Chr 8: 26.29 – 26.37 Mb	Chr 14: 67.01 – 67.07 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The product of this gene belongs to the phosphatase 2 regulatory subunit B family. Protein phosphatase 2 is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes an alpha isoform of the regulatory subunit B55 subfamily.[6]

Interactions

PPP2R2A has been shown to interact with:

• P70-S6 Kinase 1,[7][8]
• PPP2CA,[9][10]
• PPP2R1A,[11][10]
• PPP2R1B,[9][11]
• TGF beta receptor 1,[12] and
• p107.[13]

References

1. GRCh38: Ensembl release 89: ENSG00000221914 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022052 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Mayer RE, Hendrix P, Cron P, Matthies R, Stone SR, Goris J, Merlevede W, Hofsteenge J, Hemmings BA (Apr 1991). "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform". Biochemistry. 30 (15): 3589–97. doi:10.1021/bi00229a001. PMID 1849734.
6. "Entrez Gene: PPP2R2A protein phosphatase 2 (formerly 2A), regulatory subunit B, alpha isoform".
7. Peterson RT, Desai BN, Hardwick JS, Schreiber SL (Apr 1999). "Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein". Proceedings of the National Academy of Sciences of the United States of America. 96 (8): 4438–42. doi:10.1073/pnas.96.8.4438. PMC 16350. PMID 10200280.
8. Bishop JD, Nien WL, Dauphinee SM, Too CK (Aug 2006). "Prolactin activates mammalian target-of-rapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells". The Journal of Endocrinology. 190 (2): 307–12. doi:10.1677/joe.1.06368. PMID 16899564.
9. Kamibayashi C, Lickteig RL, Estes R, Walter G, Mumby MC (Oct 1992). "Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits". The Journal of Biological Chemistry. 267 (30): 21864–72. PMID 1328247.
10. Goudreault M, D'Ambrosio LM, Kean MJ, Mullin MJ, Larsen BG, Sanchez A, Chaudhry S, Chen GI, Sicheri F, Nesvizhskii AI, Aebersold R, Raught B, Gingras AC (Jan 2009). "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein". Molecular & Cellular Proteomics. 8 (1): 157–71. doi:10.1074/mcp.M800266-MCP200. PMC 2621004. PMID 18782753.
11. Zhou J, Pham HT, Ruediger R, Walter G (Jan 2003). "Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution". The Biochemical Journal. 369 (Pt 2): 387–98. doi:10.1042/BJ20021244. PMC 1223084. PMID 12370081.
12. Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R (Nov 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Molecular and Cellular Biology. 18 (11): 6595–604. doi:10.1128/mcb.18.11.6595. PMC 109244. PMID 9774674.
13. Jayadeva G, Kurimchak A, Garriga J, Sotillo E, Davis AJ, Haines DS, Mumby M, Graña X (Sep 2010). "B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activation". The Journal of Biological Chemistry. 285 (39): 29863–73. doi:10.1074/jbc.M110.162354. PMC 2943288. PMID 20663872.

Further reading

• Zolnierowicz S (Oct 2000). "Type 2A protein phosphatase, the complex regulator of numerous signaling pathways". Biochemical Pharmacology. 60 (8): 1225–35. doi:10.1016/S0006-2952(00)00424-X. PMID 11007961.
• Kino T, Pavlakis GN (Apr 2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1". DNA and Cell Biology. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377.
• Andersen JL, Planelles V (Jan 2005). "The role of Vpr in HIV-1 pathogenesis". Current HIV Research. 3 (1): 43–51. doi:10.2174/1570162052772988. PMID 15638722.
• Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology. 2: 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353.
• Kamibayashi C, Lickteig RL, Estes R, Walter G, Mumby MC (Oct 1992). "Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits". The Journal of Biological Chemistry. 267 (30): 21864–72. PMID 1328247.
• Tung HY, De Rocquigny H, Zhao LJ, Cayla X, Roques BP, Ozon R (Jan 1997). "Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr". FEBS Letters. 401 (2–3): 197–201. doi:10.1016/S0014-5793(96)01470-6. PMID 9013886.
• Ruediger R, Brewis N, Ohst K, Walter G (Nov 1997). "Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production". Virology. 238 (2): 432–43. doi:10.1006/viro.1997.8873. PMID 9400615.
• Strack S, Zaucha JA, Ebner FF, Colbran RJ, Wadzinski BE (Mar 1998). "Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits". The Journal of Comparative Neurology. 392 (4): 515–27. doi:10.1002/(SICI)1096-9861(19980323)392:4<515::AID-CNE8>3.0.CO;2-3. PMID 9514514.
• Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R (Nov 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Molecular and Cellular Biology. 18 (11): 6595–604. doi:10.1128/mcb.18.11.6595. PMC 109244. PMID 9774674.
• Ruediger R, Fields K, Walter G (Jan 1999). "Binding specificity of protein phosphatase 2A core enzyme for regulatory B subunits and T antigens". Journal of Virology. 73 (1): 839–42. PMC 103900. PMID 9847399.
• Kim ST, Lim DS, Canman CE, Kastan MB (Dec 1999). "Substrate specificities and identification of putative substrates of ATM kinase family members". The Journal of Biological Chemistry. 274 (53): 37538–43. doi:10.1074/jbc.274.53.37538. PMID 10608806.
• Moreno CS, Park S, Nelson K, Ashby D, Hubalek F, Lane WS, Pallas DC (Feb 2000). "WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A". The Journal of Biological Chemistry. 275 (8): 5257–63. doi:10.1074/jbc.275.8.5257. PMC 3505218. PMID 10681496.
• Husi H, Ward MA, Choudhary JS, Blackstock WP, Grant SG (Jul 2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nature Neuroscience. 3 (7): 661–9. doi:10.1038/76615. hdl:1842/742. PMID 10862698.
• Vogelsberg-Ragaglia V, Schuck T, Trojanowski JQ, Lee VM (Apr 2001). "PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus". Experimental Neurology. 168 (2): 402–12. doi:10.1006/exnr.2001.7630. PMID 11259128.
• Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y (Sep 2001). "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. doi:10.1006/viro.2001.1007. PMID 11531413.
• Bennin DA, Don AS, Brake T, McKenzie JL, Rosenbaum H, Ortiz L, DePaoli-Roach AA, Horne MC (Jul 2002). "Cyclin G2 associates with protein phosphatase 2A catalytic and regulatory B' subunits in active complexes and induces nuclear aberrations and a G1/S phase cell cycle arrest". The Journal of Biological Chemistry. 277 (30): 27449–67. doi:10.1074/jbc.M111693200. PMID 11956189.
• Hrimech M, Yao XJ, Branton PE, Cohen EA (Jul 2002). "Human immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2A". The EMBO Journal. 21 (14): 3918. doi:10.1093/emboj/cdf420. PMC 126131. PMID 12110603.