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Volumn 499, Issue 1, 2012, Pages 1-7

PP2A holoenzymes negatively and positively regulate cell cycle progression by dephosphorylating pocket proteins and multiple CDK substrates

Author keywords

B55alpha; E2F; P107; P130; PRB; Retinoblastoma

Indexed keywords

BONE MORPHOGENETIC PROTEIN; CELL CYCLE PROTEIN 6; CELL EXTRACT; CYCLIN DEPENDENT KINASE; FIBROBLAST GROWTH FACTOR 1; HOLOENZYME; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN SERINE THREONINE KINASE; RAF PROTEIN; RETINOIC ACID; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; WNT PROTEIN;

EID: 84859774713     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.02.015     Document Type: Review
Times cited : (47)

References (63)
  • 1
    • 30044452600 scopus 로고    scopus 로고
    • Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes
    • Adams D.G., Coffee R.L., Zhang H., Pelech S., Strack S., Wadzinski B.E. Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes. J. Biol. Chem. 2005, 280:42644-42654.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42644-42654
    • Adams, D.G.1    Coffee, R.L.2    Zhang, H.3    Pelech, S.4    Strack, S.5    Wadzinski, B.E.6
  • 2
    • 34547436948 scopus 로고    scopus 로고
    • 2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A
    • 2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:9876-9881.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9876-9881
    • Ahn, J.H.1
  • 3
    • 66849138206 scopus 로고    scopus 로고
    • PP2A regulates BMP signalling by interacting with BMP receptor complexes and by dephosphorylating both the C-terminus and the linker region of Smad1
    • Bengtsson L., Schwappacher R., Roth M., Boergermann J.H., Hassel S., Knaus P. PP2A regulates BMP signalling by interacting with BMP receptor complexes and by dephosphorylating both the C-terminus and the linker region of Smad1. J. Cell Sci. 2009, 122:1248-1257.
    • (2009) J. Cell Sci. , vol.122 , pp. 1248-1257
    • Bengtsson, L.1    Schwappacher, R.2    Roth, M.3    Boergermann, J.H.4    Hassel, S.5    Knaus, P.6
  • 4
    • 0038708117 scopus 로고    scopus 로고
    • SKP2 associates with p130 and accelerates p130 ubiquitylation and degradation in human cells
    • Bhattacharya S., Garriga J., Calbo J., Yong T., Haines D.S., Graña X. SKP2 associates with p130 and accelerates p130 ubiquitylation and degradation in human cells. Oncogene 2003, 22:2443-2451.
    • (2003) Oncogene , vol.22 , pp. 2443-2451
    • Bhattacharya, S.1    Garriga, J.2    Calbo, J.3    Yong, T.4    Haines, D.S.5    Graña, X.6
  • 5
    • 0037184608 scopus 로고    scopus 로고
    • G1 cyclin/CDK coordinated phosphorylation of endogenous pocket proteins differentially regulates their interactions with E2F4 and E2F1 and gene expression
    • Calbó J., et al. G1 cyclin/CDK coordinated phosphorylation of endogenous pocket proteins differentially regulates their interactions with E2F4 and E2F1 and gene expression. J. Biol. Chem. 2002, 277:50263-50274.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50263-50274
    • Calbó, J.1
  • 6
    • 73949151141 scopus 로고    scopus 로고
    • The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta, a phosphatase directed against CDK phosphosites
    • Castilho P.V., Williams B.C., Mochida S., Zhao Y., Goldberg M.L. The M phase kinase Greatwall (Gwl) promotes inactivation of PP2A/B55delta, a phosphatase directed against CDK phosphosites. Mol. Biol. Cell 2009, 20:4777-4789.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4777-4789
    • Castilho, P.V.1    Williams, B.C.2    Mochida, S.3    Zhao, Y.4    Goldberg, M.L.5
  • 7
    • 0037067653 scopus 로고    scopus 로고
    • E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression
    • Chen C.R., Kang Y., Siegel P.M., Massague J. E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression. Cell 2002, 110:19-32.
    • (2002) Cell , vol.110 , pp. 19-32
    • Chen, C.R.1    Kang, Y.2    Siegel, P.M.3    Massague, J.4
  • 8
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho U.S., Xu W. Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 2007, 445:53-57.
    • (2007) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.2
  • 9
    • 0038482115 scopus 로고    scopus 로고
    • Oxidative stress induces PP2A-dependent de-phosphorylation of the pocket proteins pRb, p107 and p130
    • Cicchillitti L., Fasanaro P., Biglioli P., Capogrossi M.C., Martelli F. Oxidative stress induces PP2A-dependent de-phosphorylation of the pocket proteins pRb, p107 and p130. J. Biol. Chem. 2003, 278:19509-19517.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19509-19517
    • Cicchillitti, L.1    Fasanaro, P.2    Biglioli, P.3    Capogrossi, M.C.4    Martelli, F.5
  • 10
    • 9444242683 scopus 로고    scopus 로고
    • Shared role of the pRb-related p130 and p107 proteins in limb development
    • Cobrinik D., et al. Shared role of the pRb-related p130 and p107 proteins in limb development. Genes Dev. 1996, 10:1633-1644.
    • (1996) Genes Dev. , vol.10 , pp. 1633-1644
    • Cobrinik, D.1
  • 11
    • 13244255645 scopus 로고    scopus 로고
    • PR72, a novel regulator of Wnt signaling required for Naked cuticle function
    • Creyghton M.P., et al. PR72, a novel regulator of Wnt signaling required for Naked cuticle function. Genes Dev. 2005, 19:376-386.
    • (2005) Genes Dev. , vol.19 , pp. 376-386
    • Creyghton, M.P.1
  • 13
    • 0038491622 scopus 로고    scopus 로고
    • A network of transcriptional and signaling events is activated by FGF to induce chondrocyte growth arrest and differentiation
    • Dailey L., Laplantine E., Priore R., Basilico C. A network of transcriptional and signaling events is activated by FGF to induce chondrocyte growth arrest and differentiation. J. Cell Biol. 2003, 161:1053-1066.
    • (2003) J. Cell Biol. , vol.161 , pp. 1053-1066
    • Dailey, L.1    Laplantine, E.2    Priore, R.3    Basilico, C.4
  • 14
    • 47049088633 scopus 로고    scopus 로고
    • Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit
    • Davis A.J., Yan Z., Martinez B., Mumby M.C. Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit. J. Biol. Chem. 2008, 283:16104-16114.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16104-16114
    • Davis, A.J.1    Yan, Z.2    Martinez, B.3    Mumby, M.C.4
  • 16
    • 0036932939 scopus 로고    scopus 로고
    • Protein phosphatase 1 binds strongly to the retinoblastoma protein but not to p107 or p130 in vitro and in vivo
    • Dunaief J.L., et al. Protein phosphatase 1 binds strongly to the retinoblastoma protein but not to p107 or p130 in vitro and in vivo. Curr. Eye Res. 2002, 24:392-396.
    • (2002) Curr. Eye Res. , vol.24 , pp. 392-396
    • Dunaief, J.L.1
  • 17
    • 0027251721 scopus 로고
    • The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit
    • Durfee T., et al. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 1993, 7:555-569.
    • (1993) Genes Dev. , vol.7 , pp. 555-569
    • Durfee, T.1
  • 19
    • 37749015044 scopus 로고    scopus 로고
    • A RNA interference screen identifies the protein phosphatase 2A subunit PR55gamma as a stress-sensitive inhibitor of c-SRC
    • Eichhorn P.J., Creyghton M.P., Wilhelmsen K., van Dam H., Bernards R. A RNA interference screen identifies the protein phosphatase 2A subunit PR55gamma as a stress-sensitive inhibitor of c-SRC. PLoS Genet. 2007, 3:e218.
    • (2007) PLoS Genet. , vol.3
    • Eichhorn, P.J.1    Creyghton, M.P.2    Wilhelmsen, K.3    van Dam, H.4    Bernards, R.5
  • 20
    • 13944277105 scopus 로고    scopus 로고
    • A Dynamic Equilibrium Between CDKs and PP2A Modulates Phosphorylation of pRB, p107 and p130
    • Garriga J., et al. A Dynamic Equilibrium Between CDKs and PP2A Modulates Phosphorylation of pRB, p107 and p130. Cell Cycle 2004, 3.
    • (2004) Cell Cycle , vol.3
    • Garriga, J.1
  • 21
    • 78650381938 scopus 로고    scopus 로고
    • The substrate of Greatwall kinase, Arpp 19, controls mitosis by inhibiting protein phosphatase 2A
    • Gharbi-Ayachi A., et al. The substrate of Greatwall kinase, Arpp 19, controls mitosis by inhibiting protein phosphatase 2A. Science 2010, 330:1673-1677.
    • (2010) Science , vol.330 , pp. 1673-1677
    • Gharbi-Ayachi, A.1
  • 22
    • 46749090395 scopus 로고    scopus 로고
    • Downregulation of the phosphatase nuclear targeting subunit (PNUTS) triggers pRB dephosphorylation and apoptosis in pRB positive tumor cell lines
    • Graña X. Downregulation of the phosphatase nuclear targeting subunit (PNUTS) triggers pRB dephosphorylation and apoptosis in pRB positive tumor cell lines. Cancer Biol. Ther. 2008, 7:842-844.
    • (2008) Cancer Biol. Ther. , vol.7 , pp. 842-844
    • Graña, X.1
  • 23
    • 0031741865 scopus 로고    scopus 로고
    • Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A
    • Griswold-Prenner I., Kamibayashi C., Maruoka E.M., Mumby M.C., Derynck R. Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A. Mol. Cell. Biol. 1998, 18:6595-6604.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6595-6604
    • Griswold-Prenner, I.1    Kamibayashi, C.2    Maruoka, E.M.3    Mumby, M.C.4    Derynck, R.5
  • 24
    • 0027279893 scopus 로고
    • Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing
    • Hendrix P., et al. Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A. Evidence for different size forms produced by alternative splicing. J. Biol. Chem. 1993, 268:15267-15276.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15267-15276
    • Hendrix, P.1
  • 26
    • 0031555896 scopus 로고    scopus 로고
    • CDNA cloning of a novel B subunit of Xenopus protein phosphatase 2A and its biological activity in oocytes
    • Iwashita J., Shima H., Nagao M., Sagata N. cDNA cloning of a novel B subunit of Xenopus protein phosphatase 2A and its biological activity in oocytes. Biochem. Biophys. Res. Commun. 1997, 232:218-222.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 218-222
    • Iwashita, J.1    Shima, H.2    Nagao, M.3    Sagata, N.4
  • 27
    • 0038532312 scopus 로고    scopus 로고
    • 2+-binding EF-hand motifs in the B″/PR72 subunit of protein phosphatase 2A
    • 2+-binding EF-hand motifs in the B″/PR72 subunit of protein phosphatase 2A. J. Biol. Chem. 2003, 278:10697-10706.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10697-10706
    • Janssens, V.1
  • 28
    • 77956901785 scopus 로고    scopus 로고
    • B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activation
    • Jayadeva G., et al. B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activation. J. Biol. Chem. 2010, 285:29863-29873.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29863-29873
    • Jayadeva, G.1
  • 29
    • 55349128561 scopus 로고    scopus 로고
    • PP2A-mediated dephosphorylation of p107 plays a critical role in chondrocyte cell cycle arrest by FGF
    • Kolupaeva V., Laplantine E., Basilico C. PP2A-mediated dephosphorylation of p107 plays a critical role in chondrocyte cell cycle arrest by FGF. PLoS One 2008, 3:e3447.
    • (2008) PLoS One , vol.3
    • Kolupaeva, V.1    Laplantine, E.2    Basilico, C.3
  • 30
    • 0036668467 scopus 로고    scopus 로고
    • MCM3-binding GANP DNA-primase is associated with a novel phosphatase component G5PR
    • Kono Y., et al. MCM3-binding GANP DNA-primase is associated with a novel phosphatase component G5PR. Genes Cells 2002, 7:821-834.
    • (2002) Genes Cells , vol.7 , pp. 821-834
    • Kono, Y.1
  • 31
    • 0030970366 scopus 로고    scopus 로고
    • Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes
    • Lacy S., Whyte P. Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes. Oncogene 1997, 14:2395-2406.
    • (1997) Oncogene , vol.14 , pp. 2395-2406
    • Lacy, S.1    Whyte, P.2
  • 32
    • 0037135987 scopus 로고    scopus 로고
    • FGF signaling targets the pRb-related p107 and p130 proteins to induce chondrocyte growth arrest
    • Laplantine E., Rossi F., Sahni M., Basilico C., Cobrinik D. FGF signaling targets the pRb-related p107 and p130 proteins to induce chondrocyte growth arrest. J. Cell Biol. 2002, 158:741-750.
    • (2002) J. Cell Biol. , vol.158 , pp. 741-750
    • Laplantine, E.1    Rossi, F.2    Sahni, M.3    Basilico, C.4    Cobrinik, D.5
  • 33
  • 36
    • 78650004841 scopus 로고    scopus 로고
    • Targeting mitotic exit leads to tumor regression in vivo: modulation by Cdk1, Mastl, and the PP2A/B55alpha, delta phosphatase
    • Manchado E., et al. Targeting mitotic exit leads to tumor regression in vivo: modulation by Cdk1, Mastl, and the PP2A/B55alpha, delta phosphatase. Cancer Cell 2010, 18:641-654.
    • (2010) Cancer Cell , vol.18 , pp. 641-654
    • Manchado, E.1
  • 37
    • 70349210060 scopus 로고    scopus 로고
    • Regulated activity of PP2A-B55 delta is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts
    • Mochida S., Ikeo S., Gannon J., Hunt T. Regulated activity of PP2A-B55 delta is crucial for controlling entry into and exit from mitosis in Xenopus egg extracts. EMBO J. 2009, 28:2777-2785.
    • (2009) EMBO J. , vol.28 , pp. 2777-2785
    • Mochida, S.1    Ikeo, S.2    Gannon, J.3    Hunt, T.4
  • 38
    • 78650366525 scopus 로고    scopus 로고
    • Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis
    • Mochida S., Maslen S.L., Skehel M., Hunt T. Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis. Science 2010, 330:1670-1673.
    • (2010) Science , vol.330 , pp. 1670-1673
    • Mochida, S.1    Maslen, S.L.2    Skehel, M.3    Hunt, T.4
  • 39
    • 0034050449 scopus 로고    scopus 로고
    • 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
    • Moreno C.S., et al. 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. J. Biol. Chem. 2000, 275:5257-5263.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5257-5263
    • Moreno, C.S.1
  • 40
    • 0031058041 scopus 로고    scopus 로고
    • High molecular weight protein phosphatase type 1 dephosphorylates the retinoblastoma protein
    • Nelson D.A., Krucher N.A., Ludlow J.W. High molecular weight protein phosphatase type 1 dephosphorylates the retinoblastoma protein. J. Biol. Chem. 1997, 272:4528-4535.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4528-4535
    • Nelson, D.A.1    Krucher, N.A.2    Ludlow, J.W.3
  • 41
    • 0030945547 scopus 로고    scopus 로고
    • Characterization of the mitotic phase pRb-directed protein phosphatase activity
    • Nelson D.A., Ludlow J.W. Characterization of the mitotic phase pRb-directed protein phosphatase activity. Oncogene 1997, 14:2407-2415.
    • (1997) Oncogene , vol.14 , pp. 2407-2415
    • Nelson, D.A.1    Ludlow, J.W.2
  • 42
    • 30344449783 scopus 로고    scopus 로고
    • Interaction of PP2A catalytic subunit with Rb2/p130 is required for all-trans retinoic acid suppression of ovarian carcinoma cell growth
    • Purev E., Giordano A., Soprano D.R., Soprano K.J. Interaction of PP2A catalytic subunit with Rb2/p130 is required for all-trans retinoic acid suppression of ovarian carcinoma cell growth. J. Cell. Physiol. 2006, 206:495-502.
    • (2006) J. Cell. Physiol. , vol.206 , pp. 495-502
    • Purev, E.1    Giordano, A.2    Soprano, D.R.3    Soprano, K.J.4
  • 43
    • 79251501955 scopus 로고    scopus 로고
    • PP2A interaction with Rb2/p130 mediates translocation of Rb2/p130 into the nucleus in all-trans retinoic acid-treated ovarian carcinoma cells
    • Purev E., Soprano D.R., Soprano K.J. PP2A interaction with Rb2/p130 mediates translocation of Rb2/p130 into the nucleus in all-trans retinoic acid-treated ovarian carcinoma cells. J. Cell. Physiol. 2011, 226:1027-1034.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 1027-1034
    • Purev, E.1    Soprano, D.R.2    Soprano, K.J.3
  • 44
    • 77956399552 scopus 로고    scopus 로고
    • Live-cell imaging RNAi screen identifies PP2A-B55alpha and importin-beta1 as key mitotic exit regulators in human cells
    • Schmitz M.H., et al. Live-cell imaging RNAi screen identifies PP2A-B55alpha and importin-beta1 as key mitotic exit regulators in human cells. Nat. Cell Biol. 2009, 12:886-893.
    • (2009) Nat. Cell Biol. , vol.12 , pp. 886-893
    • Schmitz, M.H.1
  • 45
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: mechanism through structure
    • Shi Y. Serine/threonine phosphatases: mechanism through structure. Cell 2009, 139:468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 48
    • 34548836850 scopus 로고    scopus 로고
    • Normal regulation of Rbf1/E2f1 target genes in Drosophila type 1 protein phosphatase mutants
    • Swanhart L.M., Sanders A.N., Duronio R.J. Normal regulation of Rbf1/E2f1 target genes in Drosophila type 1 protein phosphatase mutants. Dev. Dyn. 2007, 236:2567-2577.
    • (2007) Dev. Dyn. , vol.236 , pp. 2567-2577
    • Swanhart, L.M.1    Sanders, A.N.2    Duronio, R.J.3
  • 49
    • 0037112174 scopus 로고    scopus 로고
    • The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2)
    • Tedesco D., Lukas J., Reed S.I. The pRb-related protein p130 is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2). Genes Dev. 2002, 16:2946-2957.
    • (2002) Genes Dev. , vol.16 , pp. 2946-2957
    • Tedesco, D.1    Lukas, J.2    Reed, S.I.3
  • 50
    • 0242300176 scopus 로고    scopus 로고
    • Targets of the cyclin-dependent kinase Cdk1
    • Ubersax J.A., et al. Targets of the cyclin-dependent kinase Cdk1. Nature 2003, 425:859-864.
    • (2003) Nature , vol.425 , pp. 859-864
    • Ubersax, J.A.1
  • 52
    • 61649127812 scopus 로고    scopus 로고
    • From promiscuity to precision: protein phosphatases get a makeover
    • Virshup D.M., Shenolikar S. From promiscuity to precision: protein phosphatases get a makeover. Mol. Cell 2009, 33:537-545.
    • (2009) Mol. Cell , vol.33 , pp. 537-545
    • Virshup, D.M.1    Shenolikar, S.2
  • 53
    • 0033552957 scopus 로고    scopus 로고
    • Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein
    • Voorhoeve P.M., Hijmans E.M., Bernards R. Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein. Oncogene 1999, 18:515-524.
    • (1999) Oncogene , vol.18 , pp. 515-524
    • Voorhoeve, P.M.1    Hijmans, E.M.2    Bernards, R.3
  • 55
    • 77950523935 scopus 로고    scopus 로고
    • P107 in the public eye: an Rb understudy and more
    • Wirt S.E., Sage J. p107 in the public eye: an Rb understudy and more. Cell Div. 2010, 5:9.
    • (2010) Cell Div. , vol.5 , pp. 9
    • Wirt, S.E.1    Sage, J.2
  • 56
    • 1842413645 scopus 로고    scopus 로고
    • P130 and p107 use a conserved domain to inhibit cellular cyclin-dependent kinase activity
    • Woo M.S., Sanchez I., Dynlacht B.D. p130 and p107 use a conserved domain to inhibit cellular cyclin-dependent kinase activity. Mol. Cell. Biol. 1997, 17:3566-3579.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3566-3579
    • Woo, M.S.1    Sanchez, I.2    Dynlacht, B.D.3
  • 57
    • 79960726254 scopus 로고    scopus 로고
    • Phosphatases: providing safe passage through mitotic exit
    • Wurzenberger C., Gerlich D.W. Phosphatases: providing safe passage through mitotic exit. Nat. Rev. Mol. Cell Biol. 2011, 12:469-482.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 469-482
    • Wurzenberger, C.1    Gerlich, D.W.2
  • 58
    • 52049100425 scopus 로고    scopus 로고
    • Structure of a protein phosphatase 2A holoenzyme: insights into B55-mediated Tau dephosphorylation
    • Xu Y., Chen Y., Zhang P., Jeffrey P.D., Shi Y. Structure of a protein phosphatase 2A holoenzyme: insights into B55-mediated Tau dephosphorylation. Mol. Cell 2008, 31:873-885.
    • (2008) Mol. Cell , vol.31 , pp. 873-885
    • Xu, Y.1    Chen, Y.2    Zhang, P.3    Jeffrey, P.D.4    Shi, Y.5
  • 59
    • 33845404441 scopus 로고    scopus 로고
    • Structure of the protein phosphatase 2A holoenzyme
    • Xu Y., et al. Structure of the protein phosphatase 2A holoenzyme. Cell 2006, 127:1239-1251.
    • (2006) Cell , vol.127 , pp. 1239-1251
    • Xu, Y.1
  • 60
    • 0033972224 scopus 로고    scopus 로고
    • PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells
    • Yan Z., Fedorov S.A., Mumby M.C., Williams R.S. PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells. Mol. Cell. Biol. 2000, 20:1021-1029.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1021-1029
    • Yan, Z.1    Fedorov, S.A.2    Mumby, M.C.3    Williams, R.S.4
  • 61
    • 69249100506 scopus 로고    scopus 로고
    • PR55 alpha, a regulatory subunit of PP2A, specifically regulates PP2A-mediated beta-catenin dephosphorylation
    • Zhang W., et al. PR55 alpha, a regulatory subunit of PP2A, specifically regulates PP2A-mediated beta-catenin dephosphorylation. J. Biol. Chem. 2009, 284:22649-22656.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22649-22656
    • Zhang, W.1
  • 62
    • 0029026176 scopus 로고
    • The pRB-related protein p107 contains two growth suppression domains: independent interactions with E2F and cyclin/cdk complexes
    • Zhu L., Enders G., Lees J.A., Beijersbergen R.L., Bernards R., Harlow E. The pRB-related protein p107 contains two growth suppression domains: independent interactions with E2F and cyclin/cdk complexes. EMBO J. 1995, 14:1904-1913.
    • (1995) EMBO J. , vol.14 , pp. 1904-1913
    • Zhu, L.1    Enders, G.2    Lees, J.A.3    Beijersbergen, R.L.4    Bernards, R.5    Harlow, E.6
  • 63
    • 0028983384 scopus 로고
    • P107 uses a p21CIP1-related domain to bind cyclin/cdk2 and regulate interactions with E2F
    • Zhu L., Harlow E., Dynlacht B.D. p107 uses a p21CIP1-related domain to bind cyclin/cdk2 and regulate interactions with E2F. Genes Dev. 1995, 9:1740-1752.
    • (1995) Genes Dev. , vol.9 , pp. 1740-1752
    • Zhu, L.1    Harlow, E.2    Dynlacht, B.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.