메뉴 건너뛰기




Volumn 103, Issue 4, 2008, Pages 1309-1325

A PP2A active site mutant impedes growth and causes misregulation of native catalytic subunit expression

Author keywords

Catalytic site mutant; G1 phase delay; Protein phosphatase 2A; Regulated protein turnover

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEASOME;

EID: 40349114503     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.21514     Document Type: Article
Times cited : (2)

References (56)
  • 1
    • 33645232372 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulatory subunit B56alpha associates with c-myc and negatively regulates c-myc accumulation
    • Arnold HK, Sears RC. 2006. Protein phosphatase 2A regulatory subunit B56alpha associates with c-myc and negatively regulates c-myc accumulation. Mol Cell Biol 26:2832-2844.
    • (2006) Mol Cell Biol , vol.26 , pp. 2832-2844
    • Arnold, H.K.1    Sears, R.C.2
  • 2
    • 0032563209 scopus 로고    scopus 로고
    • Autoregulation of protein phosphatase type 2A expression
    • Baharians Z, Schönthal AH. 1998. Autoregulation of protein phosphatase type 2A expression. J Biol Chem 273:19019-19024.
    • (1998) J Biol Chem , vol.273 , pp. 19019-19024
    • Baharians, Z.1    Schönthal, A.H.2
  • 4
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type 2A by tyrosine phosphorylation
    • Chen J, Martin BL, Brautigan DL. 1992. Regulation of protein serine-threonine phosphatase type 2A by tyrosine phosphorylation. Science 257:1261-1264.
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 5
    • 0028237871 scopus 로고
    • Protein tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts
    • Chen J, Parsons S, Brautigan DL. 1994. Protein tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts. J Biol Chem 269:7957-7962.
    • (1994) J Biol Chem , vol.269 , pp. 7957-7962
    • Chen, J.1    Parsons, S.2    Brautigan, D.L.3
  • 7
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho US, Xu W. 2007. Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445:53-57.
    • (2007) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.2
  • 8
    • 0037174861 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulates binding of Cdc45 to the prereplication complex
    • Chou DM, Petersen P, Walter JC, Walter G. 2002. Protein phosphatase 2A regulates binding of Cdc45 to the prereplication complex. J Biol Chem 277:40520-40527.
    • (2002) J Biol Chem , vol.277 , pp. 40520-40527
    • Chou, D.M.1    Petersen, P.2    Walter, J.C.3    Walter, G.4
  • 9
    • 34248369400 scopus 로고    scopus 로고
    • The Yin and Yang of centromeric cohesion of sister chromatids: Mitotic kinases meet protein phosphatase 2A
    • Dai W, Wang X. 2006. The Yin and Yang of centromeric cohesion of sister chromatids: Mitotic kinases meet protein phosphatase 2A. Cell Div 1:9.
    • (2006) Cell Div , vol.1 , pp. 9
    • Dai, W.1    Wang, X.2
  • 10
    • 0035895604 scopus 로고    scopus 로고
    • Regulation of the G1 to S transition by the ubiquitin pathway
    • DeSalle LM, Pagano M. 2001. Regulation of the G1 to S transition by the ubiquitin pathway. FEBS Lett 490: 179-189.
    • (2001) FEBS Lett , vol.490 , pp. 179-189
    • DeSalle, L.M.1    Pagano, M.2
  • 11
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
    • Di Como CJ, Arndt KT. 1996. Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev 10:1904-1916.
    • (1996) Genes Dev , vol.10 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 12
    • 0033588166 scopus 로고    scopus 로고
    • Functional expression of human PP2Ac in yeast permits the identification of novel C-terminal and dominant-negative mutant forms
    • Evans DR, Myles T, Hofsteenge J, Hemmings BA. 1999. Functional expression of human PP2Ac in yeast permits the identification of novel C-terminal and dominant-negative mutant forms. J Biol Chem 274:24038-24046.
    • (1999) J Biol Chem , vol.274 , pp. 24038-24046
    • Evans, D.R.1    Myles, T.2    Hofsteenge, J.3    Hemmings, B.A.4
  • 13
    • 0021381028 scopus 로고    scopus 로고
    • Feinberg AP, Vogelstein B. 1984. A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity. Addendum. Anal Biochem 137:266-267.
    • Feinberg AP, Vogelstein B. 1984. A technique for radio-labeling DNA restriction endonuclease fragments to high specific activity. Addendum. Anal Biochem 137:266-267.
  • 14
    • 0041820233 scopus 로고    scopus 로고
    • A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo
    • Fellner T, Lackner DH, Hombauer H, Piribauer P, Mudrak I, Zaragoza K, Juno C, Ogris E. 2003. A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo. Genes Dev 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
  • 15
    • 20444485337 scopus 로고    scopus 로고
    • A novel assay for protein phosphatase 2A (PP2A) complexes in vivo reveals differential effects of covalent modifications on different Saccharomyces cerevisiae PP2A heterotrimers
    • Gentry MS, Li Y, Wei H, Syed FF, Patel SH, Hallberg RL, Pallas DC. 2005. A novel assay for protein phosphatase 2A (PP2A) complexes in vivo reveals differential effects of covalent modifications on different Saccharomyces cerevisiae PP2A heterotrimers. Eukaryot Cell 4:1029-1040.
    • (2005) Eukaryot Cell , vol.4 , pp. 1029-1040
    • Gentry, M.S.1    Li, Y.2    Wei, H.3    Syed, F.F.4    Patel, S.H.5    Hallberg, R.L.6    Pallas, D.C.7
  • 16
    • 0032946279 scopus 로고    scopus 로고
    • Protein phosphatase 2A: Who shall regulate the regulator?
    • Goldberg Y. 1999. Protein phosphatase 2A: Who shall regulate the regulator? Biochem Pharmacol 57:321-328.
    • (1999) Biochem Pharmacol , vol.57 , pp. 321-328
    • Goldberg, Y.1
  • 17
    • 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. 1999. The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell 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
  • 18
    • 0027477103 scopus 로고
    • Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A
    • Guo H, Damuni Z. 1993. Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A. Proc Natl Acad Sci USA 90:2500-2504.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2500-2504
    • Guo, H.1    Damuni, Z.2
  • 19
    • 0028901087 scopus 로고
    • Molecular cloning of a cDNA clone encoding a phosphoprotein component related to the Ig receptor-mediated signal transduction
    • Inui S, Kuwahara K, Mizutani J, Maeda K, Kawai T, Nakayasu H, Sakaguchi N. 1995. Molecular cloning of a cDNA clone encoding a phosphoprotein component related to the Ig receptor-mediated signal transduction. J Immunol 154:2714-2723.
    • (1995) J Immunol , vol.154 , pp. 2714-2723
    • Inui, S.1    Kuwahara, K.2    Mizutani, J.3    Maeda, K.4    Kawai, T.5    Nakayasu, H.6    Sakaguchi, N.7
  • 20
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling
    • Janssens V, Goris J. 2001. Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling. Biochem J 353: 417-439.
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 22
    • 0026788470 scopus 로고
    • Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits
    • Kamibayashi C, Lickteig RL, Estes R, Walter G, Mumby MC. 1992. Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits. J Biol Chem 267:21864-21872.
    • (1992) J Biol Chem , vol.267 , pp. 21864-21872
    • Kamibayashi, C.1    Lickteig, R.L.2    Estes, R.3    Walter, G.4    Mumby, M.C.5
  • 23
    • 12444268260 scopus 로고    scopus 로고
    • Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2A family (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein
    • Kloeker S, Reed R, McConnell JL, Chang D, Tran K, Westphal RS, Law BK, Colbran RJ, Kamoun M, Campbell KS, Wadzinski BE. 2003. Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2A family (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein. Protein Expr Purif 31:19-33.
    • (2003) Protein Expr Purif , vol.31 , pp. 19-33
    • Kloeker, S.1    Reed, R.2    McConnell, J.L.3    Chang, D.4    Tran, K.5    Westphal, R.S.6    Law, B.K.7    Colbran, R.J.8    Kamoun, M.9    Campbell, K.S.10    Wadzinski, B.E.11
  • 24
    • 0026018749 scopus 로고
    • INH, a negative regulator of MPF, is a form of protein phosphatase 2A
    • Lee TH, Solomon MJ, Mumby MC, Kirschner MW. 1991. INH, a negative regulator of MPF, is a form of protein phosphatase 2A. Cell 64:415-423.
    • (1991) Cell , vol.64 , pp. 415-423
    • Lee, T.H.1    Solomon, M.J.2    Mumby, M.C.3    Kirschner, M.W.4
  • 26
    • 0035811068 scopus 로고    scopus 로고
    • Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4
    • Liu J, Prickett TD, Elliott E, Meroni G, Brautigan DL. 2001. Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4. Proc Natl Acad Sci USA 98:6650-6655.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6650-6655
    • Liu, J.1    Prickett, T.D.2    Elliott, E.3    Meroni, G.4    Brautigan, D.L.5
  • 27
    • 0033007250 scopus 로고    scopus 로고
    • Functional expression of human and Arabidopsis protein phosphatase 2A in Saccharomyces cerevisiae and isolation of dominant-defective mutants
    • Lizotte DL, McManus DD, Cohen HR, DeLong A. 1999. Functional expression of human and Arabidopsis protein phosphatase 2A in Saccharomyces cerevisiae and isolation of dominant-defective mutants. Gene 234:35-44.
    • (1999) Gene , vol.234 , pp. 35-44
    • Lizotte, D.L.1    McManus, D.D.2    Cohen, H.R.3    DeLong, A.4
  • 30
    • 0035942483 scopus 로고    scopus 로고
    • A new role for protein methylation: Switching partners at the phosphatase ball
    • Mumby M. 2001. A new role for protein methylation: Switching partners at the phosphatase ball. Sci STKE 79:PE1.
    • (2001) Sci STKE , vol.79
    • Mumby, M.1
  • 31
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
    • Mumby MC, Walter G. 1993. Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth. Physiol Rev 73:673-699.
    • (1993) Physiol Rev , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 32
    • 0030984108 scopus 로고    scopus 로고
    • B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • Murata K, Wu J, Brautigan DL. 1997. 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) Proc Natl Acad Sci USA , vol.94 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 33
    • 0035395687 scopus 로고    scopus 로고
    • Active-site mutations impairing the catalytic function of the catalytic subunit of human protein phosphatase 2A permit baculovirus-mediated overexpression in insect cells
    • Myles T, Schmidt K, Evans DR, Cron P, Hemmings BA. 2001. Active-site mutations impairing the catalytic function of the catalytic subunit of human protein phosphatase 2A permit baculovirus-mediated overexpression in insect cells. Biochem J 357:225-232.
    • (2001) Biochem J , vol.357 , pp. 225-232
    • Myles, T.1    Schmidt, K.2    Evans, D.R.3    Cron, P.4    Hemmings, B.A.5
  • 35
    • 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. 1997. Protein phosphatase 2A subunit assembly: The catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen. Oncogene 15:911-917.
    • (1997) Oncogene , vol.15 , pp. 911-917
    • Ogris, E.1    Gibson, D.M.2    Pallas, D.C.3
  • 36
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    • Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC. 1999a. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J Biol Chem 274:14382-14391.
    • (1999) J Biol Chem , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6    Pallas, D.C.7
  • 37
    • 0032865617 scopus 로고    scopus 로고
    • Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src)
    • Ogris E, Mudrak I, Mak E, Gibson D, Pallas DC. 1999b. Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src). J Virol 73:7390-7398.
    • (1999) J Virol , vol.73 , pp. 7390-7398
    • Ogris, E.1    Mudrak, I.2    Mak, E.3    Gibson, D.4    Pallas, D.C.5
  • 38
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear WS, Nolan GP, Scott ML, Baltimore D. 1993. Production of high-titer helper-free retroviruses by transient transfection. Proc Natl Acad Sci USA 90: 8392-8396.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 39
    • 0034687086 scopus 로고    scopus 로고
    • Effects of regulatory subunits on the kinetics of protein phosphatase 2A
    • Price NE, Mumby MC. 2000. Effects of regulatory subunits on the kinetics of protein phosphatase 2A. Biochemistry 39:11312-11318.
    • (2000) Biochemistry , vol.39 , pp. 11312-11318
    • Price, N.E.1    Mumby, M.C.2
  • 40
    • 4644360207 scopus 로고    scopus 로고
    • Overlapping binding sites in protein phosphatase 2A for association with regulatory A and alpha-4 (mTap42) subunits
    • Prickett TD, Brautigan DL. 2004. Overlapping binding sites in protein phosphatase 2A for association with regulatory A and alpha-4 (mTap42) subunits. J Biol Chem 279:38912-38920.
    • (2004) J Biol Chem , vol.279 , pp. 38912-38920
    • Prickett, T.D.1    Brautigan, D.L.2
  • 43
    • 0026661827 scopus 로고
    • Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus
    • Ruediger R, Roeckel D, Fait J, Bergqvist A, Magnusson G, Walter G. 1992. Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus. Mol Cell Biol 12:4872-4882.
    • (1992) Mol Cell Biol , vol.12 , pp. 4872-4882
    • Ruediger, R.1    Roeckel, D.2    Fait, J.3    Bergqvist, A.4    Magnusson, G.5    Walter, G.6
  • 45
    • 0037341483 scopus 로고    scopus 로고
    • Loss of protooncogene c-Myc function impedes G1 phase progression both before and after the restriction point
    • Schorl C, Sedivy JM. 2003. Loss of protooncogene c-Myc function impedes G1 phase progression both before and after the restriction point. Mol Biol Cell 14:823-835.
    • (2003) Mol Biol Cell , vol.14 , pp. 823-835
    • Schorl, C.1    Sedivy, J.M.2
  • 46
    • 0027546848 scopus 로고
    • Effects of c-myc expression on proliferation, quiescence, and the G0 to G1 transition in nontransformed cells
    • Shichiri M, Hanson KD, Sedivy JM. 1993. Effects of c-myc expression on proliferation, quiescence, and the G0 to G1 transition in nontransformed cells. Cell Growth Differ 4:93-104.
    • (1993) Cell Growth Differ , vol.4 , pp. 93-104
    • Shichiri, M.1    Hanson, K.D.2    Sedivy, J.M.3
  • 47
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
    • Sontag E, Fedorov S, Kamibayashi C, Robbins D, Cobb M, Mumby M. 1993. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell 75: 887-897.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamibayashi, C.3    Robbins, D.4    Cobb, M.5    Mumby, M.6
  • 49
    • 0030874269 scopus 로고    scopus 로고
    • Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65alpha
    • Turowski P, Favre B, Campbell KS, Lamb NJ, Hemmings BA. 1997. Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65alpha. Eur J Biochem 248:200-208.
    • (1997) Eur J Biochem , vol.248 , pp. 200-208
    • Turowski, P.1    Favre, B.2    Campbell, K.S.3    Lamb, N.J.4    Hemmings, B.A.5
  • 50
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • Virshup DM. 2000. Protein phosphatase 2A: A panoply of enzymes. Curr Opin Cell Biol 12:180-185.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 51
    • 0344824568 scopus 로고    scopus 로고
    • Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases
    • Wang H, Wang X, Jiang Y. 2003. Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases. Mol Biol Cell 14:4342-4351.
    • (2003) Mol Biol Cell , vol.14 , pp. 4342-4351
    • Wang, H.1    Wang, X.2    Jiang, Y.3
  • 52
    • 0034331296 scopus 로고    scopus 로고
    • Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo
    • Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, Broach JR. 2000. Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J 19: 5672-5681.
    • (2000) EMBO J , vol.19 , pp. 5672-5681
    • Wu, J.1    Tolstykh, T.2    Lee, J.3    Boyd, K.4    Stock, J.B.5    Broach, J.R.6
  • 55
    • 0033527642 scopus 로고    scopus 로고
    • Distinct roles for PP1 and PP2A in phosphorylation of the retinoblastoma protein. PP2a regulates the activities of G(1) cyclin-dependent kinases
    • Yan Y, Mumby MC. 1999. Distinct roles for PP1 and PP2A in phosphorylation of the retinoblastoma protein. PP2a regulates the activities of G(1) cyclin-dependent kinases. J Biol Chem 274:31917-31924.
    • (1999) J Biol Chem , vol.274 , pp. 31917-31924
    • Yan, Y.1    Mumby, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.