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Volumn 74, Issue 1, 2009, Pages 212-221

The structure of the PP2A regulatory subunit B56y: The remaining piece of the PP2A jigsaw puzzle

Author keywords

B regulatory subunits; B56; Crystal structure; Ho loenzyme assembly; PP2A regulation; PR61; Protein phosphatase

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE 2A; HOLOENZYME; PHOSPHOPROTEIN PHOSPHATASE 2; PROTEIN SUBUNIT;

EID: 58949083857     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22150     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 15044348175 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatases: Life, death, and sleeping
    • Gallego M, Virshup DM. Protein serine/threonine phosphatases: life, death, and sleeping. Curr Opin Cell Biol 2005;17:197-202.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 197-202
    • Gallego, M.1    Virshup, D.M.2
  • 2
    • 0036667397 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatases in apoptosis
    • Klumpp S, Krieglstein J. Serine/threonine protein phosphatases in apoptosis. Curr Opin Pharmacol 2002;2:458-462.
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 458-462
    • Klumpp, S.1    Krieglstein, J.2
  • 3
    • 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
  • 6
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho US, Xu WQ. 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.Q.2
  • 7
    • 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
  • 8
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2a by tyrosine phosphorylation
    • Chen J, Martin BL, Brautigan DL. Regulation of protein serine-threonine phosphatase type-2a by tyrosine phosphorylation. Science 1992;257:1261-1264.
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 9
    • 0035177048 scopus 로고    scopus 로고
    • Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Bα regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen
    • Yu XX, Du XX, Moreno CS, Green RE, Ogris E, Feng Q, Chou L, McQuoid MJ, Pallas DC. Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Bα 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.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
  • 10
    • 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 JB. 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
  • 11
    • 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 DM, Pallas DC. 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
  • 12
    • 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 JV, 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
  • 13
    • 0035100658 scopus 로고    scopus 로고
    • Protein phosphatase 2A: The Trojan Horse of cellular signaling
    • Sontag E. Protein phosphatase 2A: the Trojan Horse of cellular signaling. Cell Signal 2001;13:7-16.
    • (2001) Cell Signal , vol.13 , pp. 7-16
    • Sontag, E.1
  • 14
    • 9144223779 scopus 로고    scopus 로고
    • Critical role for protein phosphatase 2A heterotrimers in mammalian cell survival
    • Strack S, Cribbs JT, Gomez L. Critical role for protein phosphatase 2A heterotrimers in mammalian cell survival. J Biol Chem 2004;279:47732-47739.
    • (2004) J Biol Chem , vol.279 , pp. 47732-47739
    • Strack, S.1    Cribbs, J.T.2    Gomez, L.3
  • 15
    • 0037007096 scopus 로고    scopus 로고
    • Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits
    • Silverstein AM, Barrow CA, Davis AJ, Mumby MC. Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits. Proc Natl Acad Sci USA 2002;99:4221-4226.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4221-4226
    • Silverstein, A.M.1    Barrow, C.A.2    Davis, A.J.3    Mumby, M.C.4
  • 16
    • 27744512550 scopus 로고    scopus 로고
    • Distinct protein phosphatase 2A heterotrimers modulate growth factor signaling to extracellular signal-regulated kinases and Akt
    • Van Kanegan MJ, Adams DG, Wadzinski BE, Strack S. Distinct protein phosphatase 2A heterotrimers modulate growth factor signaling to extracellular signal-regulated kinases and Akt. J Biol Chem 2005;280:36029-36036.
    • (2005) J Biol Chem , vol.280 , pp. 36029-36036
    • Van Kanegan, M.J.1    Adams, D.G.2    Wadzinski, B.E.3    Strack, S.4
  • 19
    • 0033605639 scopus 로고    scopus 로고
    • Regulation of β-catenin signaling by the B56 subunit of protein phosphatase 2A
    • Seeling JM, Miller JR, Gil R, Moon RT, White R, Virshup DM. Regulation of β-catenin signaling by the B56 subunit of protein phosphatase 2A. Science 1999;283:2089-2091.
    • (1999) Science , vol.283 , pp. 2089-2091
    • Seeling, J.M.1    Miller, J.R.2    Gil, R.3    Moon, R.T.4    White, R.5    Virshup, D.M.6
  • 20
    • 0348013155 scopus 로고    scopus 로고
    • PP2A:B56ε is required for Wnt/β-catenin signaling during embryonic development
    • Yang J, Wu JL, Tan C, Klein PS. PP2A:B56ε is required for Wnt/β-catenin signaling during embryonic development. Development 2003;130:5569-5578.
    • (2003) Development , vol.130 , pp. 5569-5578
    • Yang, J.1    Wu, J.L.2    Tan, C.3    Klein, P.S.4
  • 21
    • 0036096778 scopus 로고    scopus 로고
    • B56-associated protein phosphatase 2A is required for survival and protects from apopto-sis in Drosophila melanogaster
    • Li XH, Scuderi A, Letsou A, Virshup DM. B56-associated protein phosphatase 2A is required for survival and protects from apopto-sis in Drosophila melanogaster. Mol Cell Biol 2002;22:3674-3684.
    • (2002) Mol Cell Biol , vol.22 , pp. 3674-3684
    • Li, X.H.1    Scuderi, A.2    Letsou, A.3    Virshup, D.M.4
  • 22
    • 43049121301 scopus 로고    scopus 로고
    • A tumor suppressor role for PP2A-B56α through negative regulation of c-Myc and other key oncoproteins
    • Arnold H, Sears R. A tumor suppressor role for PP2A-B56α through negative regulation of c-Myc and other key oncoproteins. Cancer Metastasis Rev 2008;27:147-158.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 147-158
    • Arnold, H.1    Sears, R.2
  • 23
    • 33645232372 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulatory subunit B56α associates with c-Myc and negatively regulates c-Myc accumulation
    • Arnold HK, Sears RC. Protein phosphatase 2A regulatory subunit B56α associates with c-Myc and negatively regulates c-Myc accumulation. Mol Cell Biol 2006;26:2832-2844.
    • (2006) Mol Cell Biol , vol.26 , pp. 2832-2844
    • Arnold, H.K.1    Sears, R.C.2
  • 24
    • 0037221975 scopus 로고    scopus 로고
    • A truncated isoform of the protein phosphatase 2A b56γ regulatory subunit may promote genetic instability and cause tumor progression
    • Ito A, Koma Y, Watabe K, Nagano T, Endo Y, Nojima H, Kitamura Y. A truncated isoform of the protein phosphatase 2A b56γ regulatory subunit may promote genetic instability and cause tumor progression. Am J Pathol 2003;162:81-91.
    • (2003) Am J Pathol , vol.162 , pp. 81-91
    • Ito, A.1    Koma, Y.2    Watabe, K.3    Nagano, T.4    Endo, Y.5    Nojima, H.6    Kitamura, Y.7
  • 25
    • 33846542682 scopus 로고    scopus 로고
    • A specific PP2A regulatory subunit. B56γ, mediates DNA damage-induced dephospho-rylation of p53 at Thr55
    • Li HH, Cai X, Shouse GP, Piluso LG, Liu XA. A specific PP2A regulatory subunit. B56γ, mediates DNA damage-induced dephospho-rylation of p53 at Thr55. Embo J 2007;26:402-411.
    • (2007) Embo J , vol.26 , pp. 402-411
    • Li, H.H.1    Cai, X.2    Shouse, G.P.3    Piluso, L.G.4    Liu, X.A.5
  • 26
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright B, Rivers AM, Audlin S, Virshup DM. The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J Biol Chem 1996;271:22081-22089.
    • (1996) J Biol Chem , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 27
    • 0033625680 scopus 로고    scopus 로고
    • The B56α regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA- dependent protein kinase PKR
    • Xu Z, Williams BRG. The B56α regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA- dependent protein kinase PKR. Mol Cell Biol 2000;20:5285-5299.
    • (2000) Mol Cell Biol , vol.20 , pp. 5285-5299
    • Xu, Z.1    Williams, B.R.G.2
  • 28
    • 33644524383 scopus 로고    scopus 로고
    • B56-containing PP2A dephos-phorylate ERK and their activity is controlled by the early gene IEX-1 and ERK
    • Letourneux C, Rocher G, Porteu F. B56-containing PP2A dephos-phorylate ERK and their activity is controlled by the early gene IEX-1 and ERK. Embo J 2006;25:727-738.
    • (2006) Embo J , vol.25 , pp. 727-738
    • Letourneux, C.1    Rocher, G.2    Porteu, F.3
  • 29
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D. The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell 1999;96:99-110.
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3    Hemmings, B.A.4    Barford, D.5
  • 30
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 1993;26:795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 32
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger TC. Automated structure solution, density modification and model building. Acta Crystallogr D 2002;58:1937-1940.
    • (2002) Acta Crystallogr D , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 33
    • 0000449646 scopus 로고
    • Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints
    • Cowtan KD, Main P. Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Crystallogr D 1993;49:148-157.
    • (1993) Acta Crystallogr D , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 34
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS. Automated protein model building combined with iterative structure refinement. Nat Struct Biol 1999;6:458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 35
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D 2004;60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolec-ular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolec-ular structures by the maximum-likelihood method. Acta Crystallogr D 1997;53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 38
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P, Robert X, Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl Acids Res 2003;31:3320-3323.
    • (2003) Nucl Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 39
    • 34249876632 scopus 로고    scopus 로고
    • Structural and biochemical insights into the regulation of protein phos-phatase 2A by small t antigen of SV40
    • Chen Y, Xu Y, BaoQ,XingY,LiZ,Lin Z, StockJB, Jeffrey PD, Shi Y. Structural and biochemical insights into the regulation of protein phos-phatase 2A by small t antigen of SV40. Nat Struct Biol 2007; 14:527-534.
    • (2007) Nat Struct Biol , vol.14 , pp. 527-534
    • Chen, Y.1    Xu, Y.2    Bao, Q.3    Xing, Y.4    Li, Z.5    Lin, Z.6    Stock, J.B.7    Jeffrey, P.D.8    Shi, Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.