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Volumn 41, Issue 3, 2011, Pages 331-342

The Structural Basis for Tight Control of PP2A Methylation and Function by LCMT-1

Author keywords

[No Author keywords available]

Indexed keywords

HOLOENZYME; LEUCINE CARBOXYL METHYLTRANSFERASE 1 (; METHYLTRANSFERASE; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; UNCLASSIFIED DRUG;

EID: 79251553753     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2010.12.030     Document Type: Article
Times cited : (103)

References (45)
  • 1
    • 27944448894 scopus 로고    scopus 로고
    • Involvement of PP2A in viral and cellular transformation
    • Arroyo J.D., Hahn W.C. Involvement of PP2A in viral and cellular transformation. Oncogene 2005, 24:7746-7755.
    • (2005) Oncogene , vol.24 , pp. 7746-7755
    • Arroyo, J.D.1    Hahn, W.C.2
  • 3
    • 0033560729 scopus 로고    scopus 로고
    • Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit
    • Bryant J.C., Westphal R.S., Wadzinski B.E. Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit. Biochem. J. 1999, 339:241-246.
    • (1999) Biochem. J. , vol.339 , pp. 241-246
    • Bryant, J.C.1    Westphal, R.S.2    Wadzinski, B.E.3
  • 5
    • 0033543158 scopus 로고    scopus 로고
    • Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2
    • Chung H., Nairn A.C., Murata K., Brautigan D.L. Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2. Biochemistry 1999, 38:10371-10376.
    • (1999) Biochemistry , vol.38 , pp. 10371-10376
    • Chung, H.1    Nairn, A.C.2    Murata, K.3    Brautigan, D.L.4
  • 6
    • 0033554835 scopus 로고    scopus 로고
    • Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue
    • De Baere I., Derua R., Janssens V., Van Hoof C., Waelkens E., Merlevede W., Goris J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry 1999, 38:16539-16547.
    • (1999) Biochemistry , vol.38 , pp. 16539-16547
    • De Baere, I.1    Derua, R.2    Janssens, V.3    Van Hoof, C.4    Waelkens, E.5    Merlevede, W.6    Goris, J.7
  • 8
    • 0028361380 scopus 로고
    • The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo
    • Favre B., Zolnierowicz S., Turowski P., Hemmings B.A. The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. J. Biol. Chem. 1994, 269:16311-16317.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16311-16317
    • Favre, B.1    Zolnierowicz, S.2    Turowski, P.3    Hemmings, B.A.4
  • 9
    • 0041820233 scopus 로고    scopus 로고
    • A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo
    • Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I., Zaragoza K., Juno C., Ogris E. A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo. Genes Dev. 2003, 17:2138-2150.
    • (2003) Genes Dev. , vol.17 , pp. 2138-2150
    • Fellner, T.1    Lackner, D.H.2    Hombauer, H.3    Piribauer, P.4    Mudrak, I.5    Zaragoza, K.6    Juno, C.7    Ogris, E.8
  • 10
    • 0028241574 scopus 로고
    • Carboxyl methylation of protein phosphatase 2A from Xenopus eggs is stimulated by cAMP and inhibited by okadaic acid
    • Floer M., Stock J. Carboxyl methylation of protein phosphatase 2A from Xenopus eggs is stimulated by cAMP and inhibited by okadaic acid. Biochem. Biophys. Res. Commun. 1994, 198:372-379.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 372-379
    • Floer, M.1    Stock, J.2
  • 11
    • 0032508379 scopus 로고    scopus 로고
    • Purification and characterization of ceramide-activated protein phosphatases
    • Galadari S., Kishikawa K., Kamibayashi C., Mumby M.C., Hannun Y.A. Purification and characterization of ceramide-activated protein phosphatases. Biochemistry 1998, 37:11232-11238.
    • (1998) Biochemistry , vol.37 , pp. 11232-11238
    • Galadari, S.1    Kishikawa, K.2    Kamibayashi, C.3    Mumby, M.C.4    Hannun, Y.A.5
  • 12
    • 0024278373 scopus 로고
    • Modulation of the substrate specificity of the polycation-stimulated protein phosphatase from Xenopus laevis oocytes
    • Hermann J., Cayla X., Dumortier K., Goris J., Ozon R., Merlevede W. Modulation of the substrate specificity of the polycation-stimulated protein phosphatase from Xenopus laevis oocytes. Eur. J. Biochem. 1988, 173:17-25.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 17-25
    • Hermann, J.1    Cayla, X.2    Dumortier, K.3    Goris, J.4    Ozon, R.5    Merlevede, W.6
  • 14
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V., Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 2001, 353:417-439.
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 1991, 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt G.J., Read R.J. Not your average density. Structure 1997, 5:1557-1569.
    • (1997) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 19
    • 70349780568 scopus 로고    scopus 로고
    • Alpha4 is an essential regulator of PP2A phosphatase activity
    • Kong M., Ditsworth D., Lindsten T., Thompson C.B. Alpha4 is an essential regulator of PP2A phosphatase activity. Mol. Cell 2009, 36:51-60.
    • (2009) Mol. Cell , vol.36 , pp. 51-60
    • Kong, M.1    Ditsworth, D.2    Lindsten, T.3    Thompson, C.B.4
  • 20
    • 35648957688 scopus 로고    scopus 로고
    • Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells
    • Lee J.A., Pallas D.C. Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells. J. Biol. Chem. 2007, 282:30974-30984.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30974-30984
    • Lee, J.A.1    Pallas, D.C.2
  • 21
    • 0027184102 scopus 로고
    • Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase
    • Lee J., Stock J. Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase. J. Biol. Chem. 1993, 268:19192-19195.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19192-19195
    • Lee, J.1    Stock, J.2
  • 23
    • 0027939868 scopus 로고
    • Okadaic acid and microcystin-LR directly inhibit the methylation of protein phosphatase 2A by its specific methyltransferase
    • Li M., Damuni Z. Okadaic acid and microcystin-LR directly inhibit the methylation of protein phosphatase 2A by its specific methyltransferase. Biochem. Biophys. Res. Commun. 1994, 202:1023-1030.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1023-1030
    • Li, M.1    Damuni, Z.2
  • 24
    • 34848843828 scopus 로고    scopus 로고
    • Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit
    • Longin S., Zwaenepoel K., Louis J.V., Dilworth S., Goris J., Janssens V. Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit. J. Biol. Chem. 2007, 282:26971-26980.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26971-26980
    • Longin, S.1    Zwaenepoel, K.2    Louis, J.V.3    Dilworth, S.4    Goris, J.5    Janssens, V.6
  • 26
    • 0035942483 scopus 로고    scopus 로고
    • A new role for protein methylation: switching partners at the phosphatase ball
    • Mumby M. A new role for protein methylation: switching partners at the phosphatase ball. Sci. STKE 2001, 79:pe1.
    • (2001) Sci. STKE , vol.79
    • Mumby, M.1
  • 28
    • 0030821233 scopus 로고    scopus 로고
    • Protein phosphatase 2A subunit assembly: the catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen
    • Ogris E., Gibson D.M., Pallas D.C. Protein phosphatase 2A subunit assembly: the catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen. Oncogene 1997, 15:911-917.
    • (1997) Oncogene , vol.15 , pp. 911-917
    • Ogris, E.1    Gibson, D.M.2    Pallas, D.C.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • Rao R.K., Clayton L.W. Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation. Biochem. Biophys. Res. Commun. 2002, 293:610-616.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 31
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf A.W., van Aalten D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:1355-1363.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    van Aalten, D.M.2
  • 32
    • 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
  • 33
    • 5644293035 scopus 로고    scopus 로고
    • Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis
    • Sontag E., Hladik C., Montgomery L., Luangpirom A., Mudrak I., Ogris E., White C.L. Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis. J. Neuropathol. Exp. Neurol. 2004, 63:1080-1091.
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , pp. 1080-1091
    • Sontag, E.1    Hladik, C.2    Montgomery, L.3    Luangpirom, A.4    Mudrak, I.5    Ogris, E.6    White, C.L.7
  • 34
    • 0034331359 scopus 로고    scopus 로고
    • Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
    • Tolstykh T., Lee J., Vafai S., Stock J.B. Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits. EMBO J. 2000, 19:5682-5691.
    • (2000) EMBO J. , vol.19 , pp. 5682-5691
    • Tolstykh, T.1    Lee, J.2    Vafai, S.3    Stock, J.B.4
  • 35
    • 0028940016 scopus 로고
    • Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression
    • Turowski P., Fernandez A., Favre B., Lamb N.J., Hemmings B.A. Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. J. Cell Biol. 1995, 129:397-410.
    • (1995) J. Cell Biol. , vol.129 , pp. 397-410
    • Turowski, P.1    Fernandez, A.2    Favre, B.3    Lamb, N.J.4    Hemmings, B.A.5
  • 36
    • 0037042211 scopus 로고    scopus 로고
    • Protein phosphatase 2A methylation: a link between elevated plasma homocysteine and Alzheimer's Disease
    • Vafai S.B., Stock J.B. Protein phosphatase 2A methylation: a link between elevated plasma homocysteine and Alzheimer's Disease. FEBS Lett. 2002, 518:1-4.
    • (2002) FEBS Lett. , vol.518 , pp. 1-4
    • Vafai, S.B.1    Stock, J.B.2
  • 37
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: a panoply of enzymes
    • Virshup D.M. Protein phosphatase 2A: a panoply of enzymes. Curr. Opin. Cell Biol. 2000, 12:180-185.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 38
    • 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
  • 39
    • 0035846951 scopus 로고    scopus 로고
    • Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p
    • Wei H., Ashby D.G., Moreno C.S., Ogris E., Yeong F.M., Corbett A.H., Pallas D.C. Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p. J. Biol. Chem. 2001, 276:1570-1577.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1570-1577
    • Wei, H.1    Ashby, D.G.2    Moreno, C.S.3    Ogris, E.4    Yeong, F.M.5    Corbett, A.H.6    Pallas, D.C.7
  • 40
    • 32344441148 scopus 로고    scopus 로고
    • Design, synthesis, and preliminary biological evaluation of a DNA methyltransferase-directed alkylating agent
    • Weller R.L., Rajski S.R. Design, synthesis, and preliminary biological evaluation of a DNA methyltransferase-directed alkylating agent. ChemBioChem 2006, 7:243-245.
    • (2006) ChemBioChem , vol.7 , pp. 243-245
    • Weller, R.L.1    Rajski, S.R.2
  • 41
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn M.D., Murshudov G.N., Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 2003, 374:300-321.
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 42
    • 0028154020 scopus 로고
    • Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain
    • Xie H., Clarke S. Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain. J. Biol. Chem. 1994, 269:1981-1984.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1981-1984
    • Xie, H.1    Clarke, S.2
  • 44
    • 41149175685 scopus 로고    scopus 로고
    • Structural mechanism of demethylation and inactivation of protein phosphatase 2A
    • Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y. Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell 2008, 133:154-163.
    • (2008) Cell , vol.133 , pp. 154-163
    • Xing, Y.1    Li, Z.2    Chen, Y.3    Stock, J.B.4    Jeffrey, P.D.5    Shi, Y.6
  • 45
    • 0035177048 scopus 로고    scopus 로고
    • Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen
    • Yu X.X., Du X., Moreno C.S., Green R.E., Ogris E., Feng Q., Chou L., McQuoid M.J., Pallas D.C. Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen. Mol. Biol. Cell 2001, 12:185-199.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 185-199
    • Yu, X.X.1    Du, X.2    Moreno, C.S.3    Green, R.E.4    Ogris, E.5    Feng, Q.6    Chou, L.7    McQuoid, M.J.8    Pallas, D.C.9


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