'''Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform''' is an [[enzyme]] that in humans is encoded by the ''PPP2R2A'' [[gene]].<ref name="pmid1849734">{{cite journal | vauthors = Mayer RE, Hendrix P, Cron P, Matthies R, Stone SR, Goris J, Merlevede W, Hofsteenge J, Hemmings BA | title = Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform | journal = Biochemistry | volume = 30 | issue = 15 | pages = 3589–97 | date = Apr 1991 | pmid = 1849734 | pmc = | doi = 10.1021/bi00229a001 }}</ref>
'''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]].<ref name="pmid1849734">{{cite journal | vauthors = Mayer RE, Hendrix P, Cron P, Matthies R, Stone SR, Goris J, Merlevede W, Hofsteenge J, Hemmings BA | title = Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform | journal = Biochemistry | volume = 30 | issue = 15 | pages = 3589–97 | date = Apr 1991 | pmid = 1849734 | pmc = | doi = 10.1021/bi00229a001 }}</ref>
Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform is an enzyme regulator that in humans is encoded by the PPP2R2Agene.[1]
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.[2]
↑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. PMID1849734.
↑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. PMID16899564.
↑ 5.05.1Kamibayashi 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. PMID1328247.
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. PMID11007961.
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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. PMID1328247.
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. PMID9013886.
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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. PMID10608806.
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. PMID10862698.
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. PMID11259128.
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. PMID11531413.
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. PMID11956189.