메뉴 건너뛰기




Volumn 4, Issue , 2013, Pages

Structural basis of protein phosphatase 2A stable latency

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA4 INTEGRIN; PHOSPHOPROTEIN PHOSPHATASE 2A;

EID: 84877727703     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2663     Document Type: Article
Times cited : (59)

References (42)
  • 1
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • DOI 10.1042/0264-6021:3530417
    • Janssens, V. & Goris, J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353, 417-439 (2001). (Pubitemid 32158309)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 2
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • DOI 10.1016/S0955-0674(99)00074-5
    • Virshup, D. M. Protein phosphatase 2A: a panoply of enzymes. Curr. Opin. Cell Biol. 12, 180-185 (2000). (Pubitemid 30142564)
    • (2000) Current Opinion in Cell Biology , vol.12 , Issue.2 , pp. 180-185
    • Virshup, D.M.1
  • 3
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
    • Di Como, C. J. & Arndt, K. T. Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev. 10, 1904-1916 (1996). (Pubitemid 26281685)
    • (1996) Genes and Development , vol.10 , Issue.15 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 4
    • 0030984108 scopus 로고    scopus 로고
    • B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • DOI 10.1073/pnas.94.20.10624
    • Murata, K., Wu, J. & Brautigan, D. L. B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc. Natl Acad. Sci. USA 94, 10624-10629 (1997). (Pubitemid 27430784)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.20 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 5
    • 4644360207 scopus 로고    scopus 로고
    • Overlapping binding sites in protein phosphatase 2A for association with regulatory A and α-4 (mTap42) subunits
    • DOI 10.1074/jbc.M401444200
    • Prickett, T. D. & Brautigan, D. L. Overlapping binding sites in protein phosphatase 2A for association with regulatory A and alpha-4 (mTap42) subunits. J. Biol. Chem. 279, 38912-38920 (2004). (Pubitemid 39296052)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.37 , pp. 38912-38920
    • Prickett, T.D.1    Brautigan, D.L.2
  • 6
    • 0028901087 scopus 로고
    • Molecular cloning of a cDNA clone encoding a phosphoprotein component related to the Ig receptor-mediated signal transduction
    • Inui, S. et al. Molecular cloning of a cDNA clone encoding a phosphoprotein component related to the Ig receptor-mediated signal transduction. J. Immunol. 154, 2714-2723 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 2714-2723
    • Inui, S.1
  • 8
    • 0036165407 scopus 로고    scopus 로고
    • BCR signal through α4 is involved in S6 kinase activation and required for B cell maturation including isotype switching and V region somatic hypermutation
    • Inui, S. et al. BCR signal through alpha 4 is involved in S6 kinase activation and required for B cell maturation including isotype switching and V region somatic hypermutation. Int. Immunol. 14, 177-187 (2002). (Pubitemid 34144742)
    • (2002) International Immunology , vol.14 , Issue.2 , pp. 177-187
    • Inui, S.1    Maeda, K.2    Hua, D.R.3    Yamashita, T.4    Yamamoto, H.5    Miyamoto, E.6    Aizawa, S.7    Sakaguchi, N.8
  • 10
    • 79959829735 scopus 로고    scopus 로고
    • Alpha4 is highly expressed in carcinogen-transformed human cells and primary human cancers
    • Chen, L. P. et al. alpha4 is highly expressed in carcinogen-transformed human cells and primary human cancers. Oncogene 30, 2943-2953 (2011).
    • (2011) Oncogene , vol.30 , pp. 2943-2953
    • Chen, L.P.1
  • 11
    • 0033577745 scopus 로고    scopus 로고
    • Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast
    • DOI 10.1093/emboj/18.10.2782
    • Jiang, Y. & Broach, J. R. Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast. EMBO J. 18, 2782-2792 (1999). (Pubitemid 29233950)
    • (1999) EMBO Journal , vol.18 , Issue.10 , pp. 2782-2792
    • Jiang, Y.1    Broach, J.R.2
  • 12
    • 17344381954 scopus 로고    scopus 로고
    • Multiple roles of Tap42 in mediating rapamycin-induced transcriptional changes in yeast
    • DOI 10.1016/S1097-2765(03)00228-4
    • Duvel, K., Santhanam, A., Garrett, S., Schneper, L. & Broach, J. R. Multiple roles of Tap42 in mediating rapamycin-induced transcriptional changes in yeast. Mol. Cell 11, 1467-1478 (2003). (Pubitemid 36776534)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1467-1478
    • Duvel, K.1    Santhanam, A.2    Garrett, S.3    Schneper, L.4    Broach, J.R.5
  • 13
    • 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 36, 51-60 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 51-60
    • Kong, M.1    Ditsworth, D.2    Lindsten, T.3    Thompson, C.B.4
  • 14
    • 0033033091 scopus 로고    scopus 로고
    • Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases
    • DOI 10.1016/S0014-5793(99)00189-1, PII S0014579399001891
    • Nanahoshi, M. et al. Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases. FEBS Lett. 446, 108-112 (1999). (Pubitemid 29127259)
    • (1999) FEBS Letters , vol.446 , Issue.1 , pp. 108-112
    • Nanahoshi, M.1    Tsujishita, Y.2    Tokunaga, C.3    Inui, S.4    Sakaguchi, N.5    Hara, K.6    Yonezawa, K.7
  • 16
    • 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 38, 10371-10376 (1999).
    • (1999) Biochemistry , vol.38 , pp. 10371-10376
    • Chung, H.1    Nairn, A.C.2    Murata, K.3    Brautigan, D.L.4
  • 17
    • 2342654045 scopus 로고    scopus 로고
    • MID1 and MID2 homo-and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit alpha 4 to microtubules: Implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders
    • Short, K. M., Hopwood, B., Yi, Z. & Cox, T. C. MID1 and MID2 homo-and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders. BMC Cell Biol. 3, 1 (2002).
    • (2002) BMC Cell Biol. , vol.3 , pp. 1
    • Short, K.M.1    Hopwood, B.2    Yi, Z.3    Cox, T.C.4
  • 18
    • 77749298896 scopus 로고    scopus 로고
    • Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination
    • McConnell, J. L. et al. Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination. Biochemistry 49, 1713-1718 (2010).
    • (2010) Biochemistry , vol.49 , pp. 1713-1718
    • McConnell, J.L.1
  • 19
    • 79251553753 scopus 로고    scopus 로고
    • The structural basis for tight control of PP2A methylation and function by LCMT-1
    • Stanevich, V. et al. The structural basis for tight control of PP2A methylation and function by LCMT-1. Mol. Cell 41, 331-342 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 331-342
    • Stanevich, V.1
  • 20
    • 34547614282 scopus 로고    scopus 로고
    • The structure of Tap42/α4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation
    • DOI 10.1021/bi7007118
    • Yang, J., Roe, S. M., Prickett, T. D., Brautigan, D. L. & Barford, D. The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation. Biochemistry 46, 8807-8815 (2007). (Pubitemid 47204446)
    • (2007) Biochemistry , vol.46 , Issue.30 , pp. 8807-8815
    • Yang, J.1    Roe, S.M.2    Prickett, T.D.3    Brautigan, D.L.4    Barford, D.5
  • 21
    • 79955958006 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase-and protein phosphatase 2A (PP2A)-binding domains of the alpha4 protein are both required for alpha4 to inhibit PP2A degradation
    • Lenoue-Newton, M. et al. The E3 ubiquitin ligase-and protein phosphatase 2A (PP2A)-binding domains of the alpha4 protein are both required for alpha4 to inhibit PP2A degradation. J. Biol. Chem. 286, 17665-17671 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 17665-17671
    • Lenoue-Newton, M.1
  • 24
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G., Paige, J. S. & Jaffrey, S. R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 28, 868-873 (2010).
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 26
    • 0036096778 scopus 로고    scopus 로고
    • B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster
    • DOI 10.1128/MCB.22.11.3674-3684.2002
    • Li, X., Scuderi, A., Letsou, A. & Virshup, D. M. B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster. Mol. Cell Biol. 22, 3674-3684 (2002). (Pubitemid 34525211)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.11 , pp. 3674-3684
    • Li, X.1    Scuderi, A.2    Letsou, A.3    Virshup, D.M.4
  • 27
    • 9144223779 scopus 로고    scopus 로고
    • Critical role for protein phosphatase 2A heterotrimers in mammalian cell survival
    • DOI 10.1074/jbc.M408015200
    • Strack, S., Cribbs, J. T. & Gomez, L. Critical role for protein phosphatase 2A heterotrimers in mammalian cell survival. J. Biol. Chem. 279, 47732-47739 (2004). (Pubitemid 39540921)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47732-47739
    • Strack, S.1    Cribbs, J.T.2    Gomez, L.3
  • 29
    • 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. 269, 1981-1984 (1994). (Pubitemid 24035403)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.3 , pp. 1981-1984
    • Xie, H.1    Clarke, S.2
  • 30
    • 0027959477 scopus 로고
    • An enzymatic activity in bovine brain that catalyzes the reversal of the C-terminal methyl esterification of protein phosphatase 2A
    • DOI 10.1006/bbrc.1994.2383
    • Xie, H. & Clarke, S. An enzymatic activity in bovine brain that catalyzes the reversal of the C-terminal methyl esterification of protein phosphatase 2A. Biochem. Biophys. Res. Commun. 203, 1710-1715 (1994). (Pubitemid 24321561)
    • (1994) Biochemical and Biophysical Research Communications , vol.203 , Issue.3 , pp. 1710-1715
    • Xie, H.1    Clarke, S.2
  • 31
    • 0027504948 scopus 로고
    • Methyl esterification of C-terminal leucine residues in cytosolic 36-kDa polypeptides of bovine brain. A novel eucaryotic protein carboxyl methylation reaction
    • Xie, H. & Clarke, S. Methyl esterification of C-terminal leucine residues in cytosolic 36-kDa polypeptides of bovine brain. A novel eucaryotic protein carboxyl methylation reaction. J. Biol. Chem. 268, 13364-13371 (1993). (Pubitemid 23307760)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.18 , pp. 13364-13371
    • Xie, H.1    Clarke, S.2
  • 32
    • 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. 268, 19192-19195 (1993). (Pubitemid 23270686)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19192-19195
    • Lee, J.1    Stock, J.2
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997). (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 4644256357 scopus 로고    scopus 로고
    • Crank: New methods for automated macromolecular crystal structure solution
    • DOI 10.1016/j.str.2004.07.018, PII S0969212604002874
    • Ness, S. R., de Graaff, R. A., Abrahams, J. P. & Pannu, N. S. CRANK: new methods for automated macromolecular crystal structure solution. Structure 12, 1753-1761 (2004). (Pubitemid 39298960)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1753-1761
    • Ness, S.R.1    De Graaff, R.A.G.2    Abrahams, J.P.3    Pannu, N.S.4
  • 35
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 37
    • 4344685580 scopus 로고    scopus 로고
    • The application of multivariate statistical techniques improves single-wavelength anomalous diffraction phasing
    • DOI 10.1107/S0907444903020808
    • Pannu, N. S. & Read, R. J. The application of multivariate statistical techniques improves single-wavelength anomalous diffraction phasing. Acta Crystallogr. D Biol. Crystallogr. 60, 22-27 (2004). (Pubitemid 41308819)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.1 , pp. 22-27
    • Pannu, N.S.1    Read, R.J.2
  • 38
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • DOI 10.1107/S0907444906022116
    • Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011 (2006). (Pubitemid 44337374)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.9 , pp. 1002-1011
    • Cowtan, K.1
  • 40
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS Refinement in REFMAC at Moderate Resolutions
    • DOI 10.1016/S0076-6879(03)74014-2
    • Winn, M. D., Murshudov, G. N. & Papiz, M. Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374, 300-321 (2003). (Pubitemid 37531815)
    • (2003) Methods in Enzymology , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 41
    • 77950946245 scopus 로고    scopus 로고
    • Regulation of phenylalanine hydroxylase: Conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometry
    • Li, J., Dangott, L. J. & Fitzpatrick, P. F. Regulation of phenylalanine hydroxylase: conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometry. Biochemistry 49, 3327-3335 (2010).
    • (2010) Biochemistry , vol.49 , pp. 3327-3335
    • Li, J.1    Dangott, L.J.2    Fitzpatrick, P.F.3
  • 42
    • 33751337111 scopus 로고    scopus 로고
    • Semi-Automated Data Processing of Hydrogen Exchange Mass Spectra Using HX-Express
    • DOI 10.1016/j.jasms.2006.07.025, PII S1044030506006891
    • Weis, D. D., Engen, J. R. & Kass, I. J. Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom. 17, 1700-1703 (2006). (Pubitemid 44809951)
    • (2006) Journal of the American Society for Mass Spectrometry , vol.17 , Issue.12 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.