메뉴 건너뛰기




Volumn 458, Issue 2, 2014, Pages 213-224

Erratum: The chaperonin CCT interacts with and mediates the correct folding and activity of three subunits of translation initiation factor eIF3: b, i and h ( Roobol et al., Biochem. J. (2014) 458:2 (213–224) DOI:10.1042/BJ20130979);The chaperonin CCT interacts with and mediates the correct folding and activity of three subunits of translation initiation factor eIF3: B, i and h

Author keywords

Chaperonin containing TCP 1 (tailless complex polypeptide 1) (CCT); Cold shock; Eukaryotic initiation factor 3 (eIF3); Hypothermia; Protein folding; Translation

Indexed keywords

CHAPERONIN CONTAINING TCP1; INITIATION FACTOR 3; PROTEIN P53;

EID: 84894267444     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130979_COR     Document Type: Erratum
Times cited : (14)

References (51)
  • 3
    • 34547178178 scopus 로고    scopus 로고
    • Reconstitution reveals the functional core of mammalian eIF3
    • Matsutani, M., Sonenberg, N., Yokoyama, S. and Imataka, H. (2007) Reconstitution reveals the functional core of mammalian eIF3. EMBO J. 26, 3373-3383
    • (2007) EMBO J. , vol.26 , pp. 3373-3383
    • Matsutani, M.1    Sonenberg, N.2    Yokoyama, S.3    Imataka, H.4
  • 4
    • 0035865256 scopus 로고    scopus 로고
    • Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding
    • Valasek, L., Phan, L., Schoenfeld, L. W., Valaskova, V. and Hinnebusch, A. G. (2001) Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding. EMBO J. 20, 891-904
    • (2001) EMBO J. , vol.20 , pp. 891-904
    • Valasek, L.1    Phan, L.2    Schoenfeld, L.W.3    Valaskova, V.4    Hinnebusch, A.G.5
  • 6
    • 84863338242 scopus 로고    scopus 로고
    • Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly
    • Herrmannova, A., Daujotyte, D., Yang, J. C., Cuchalova, L., Gorrec, F., Wagner, S., Danyi, I., Lukavsky, P. J. and Valasek, L. S. (2012) Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly. Nucleic Acids Res. 40, 2294-2311
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2294-2311
    • Herrmannova, A.1    Daujotyte, D.2    Yang, J.C.3    Cuchalova, L.4    Gorrec, F.5    Wagner, S.6    Danyi, I.7    Lukavsky, P.J.8    Valasek, L.S.9
  • 7
    • 28544439977 scopus 로고    scopus 로고
    • Structural roles for human translation factor eIF3 in initiation of protein synthesis
    • Siridechadilok, B., Fraser, C. S., Hall, R. J., Doudna, J. A. and Nogales, E. (2005) Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310, 1513-1515
    • (2005) Science , vol.310 , pp. 1513-1515
    • Siridechadilok, B.1    Fraser, C.S.2    Hall, R.J.3    Doudna, J.A.4    Nogales, E.5
  • 8
    • 10644277580 scopus 로고    scopus 로고
    • Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association
    • Kolupaeva, V. G., Unbehaun, A., Lomakin, I. B., Hellen, C. U. and Pestova, T. V. (2005) Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association. RNA 11, 470-486
    • (2005) RNA , vol.11 , pp. 470-486
    • Kolupaeva, V.G.1    Unbehaun, A.2    Lomakin, I.B.3    Hellen, C.U.4    Pestova, T.V.5
  • 9
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valasek, L., Nielsen, K. H. and Hinnebusch, A. G. (2002) Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J. 21, 5886-5898
    • (2002) EMBO J. , vol.21 , pp. 5886-5898
    • Valasek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 10
  • 12
    • 34247165835 scopus 로고    scopus 로고
    • Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells
    • Zhang, L., Pan, X. and Hershey, J. W. (2007) Individual overexpression of five subunits of human translation initiation factor eIF3 promotes malignant transformation of immortal fibroblast cells. J. Biol. Chem. 282, 5790-5800
    • (2007) J. Biol. Chem. , vol.282 , pp. 5790-5800
    • Zhang, L.1    Pan, X.2    Hershey, J.W.3
  • 13
    • 33845397658 scopus 로고    scopus 로고
    • Carcinoma-associated eIF3i overexpression facilitates mTOR-dependent growth transformation
    • Ahlemann, M., Zeidler, R., Lang, S., Mack, B., Munz, M. and Gires, O. (2006) Carcinoma-associated eIF3i overexpression facilitates mTOR-dependent growth transformation. Mol. Carcinog. 45, 957-967
    • (2006) Mol. Carcinog. , vol.45 , pp. 957-967
    • Ahlemann, M.1    Zeidler, R.2    Lang, S.3    Mack, B.4    Munz, M.5    Gires, O.6
  • 14
    • 33750044299 scopus 로고    scopus 로고
    • When translation meets transformation: The mTOR story
    • Averous, J. and Proud, C. G. (2006) When translation meets transformation: the mTOR story. Oncogene 25, 6423-6435
    • (2006) Oncogene , vol.25 , pp. 6423-6435
    • Averous, J.1    Proud, C.G.2
  • 15
    • 53049108498 scopus 로고    scopus 로고
    • An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3
    • Zhang, L., Smit-McBride, Z., Pan, X., Rheinhardt, J. and Hershey, J. W. B. (2008) An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3. J. Biol. Chem. 283, 24047-24060
    • (2008) J. Biol. Chem. , vol.283 , pp. 24047-24060
    • Zhang, L.1    Smit-Mcbride, Z.2    Pan, X.3    Rheinhardt, J.4    Hershey, J.W.B.5
  • 16
    • 65349129412 scopus 로고    scopus 로고
    • Identification of the limitations on recombinant gene expression in CHO cell lines with varying luciferase production rates
    • Mead, E. J., Chiverton, L. M., Smales, C. M. and von der Haar, T. (2009) Identification of the limitations on recombinant gene expression in CHO cell lines with varying luciferase production rates. Biotechnol. Bioeng. 102, 1593-1602
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 1593-1602
    • Mead, E.J.1    Chiverton, L.M.2    Smales, C.M.3    Von Der Haar, T.4
  • 17
    • 57649187405 scopus 로고    scopus 로고
    • Biochemical insights into the mechanisms central to the response of mammalian cells to cold-stress and subsequent rewarming
    • Roobol, A., Carden, M. J., Newsam, R. J. and Smales, C. M. (2009) Biochemical insights into the mechanisms central to the response of mammalian cells to cold-stress and subsequent rewarming. FEBS J. 276, 286-302
    • FEBS J. , vol.276 , pp. 286-302
    • Roobol, A.1    Carden, M.J.2    Newsam, R.J.3    Smales, C.M.M.4
  • 18
    • 66449098776 scopus 로고    scopus 로고
    • Cold-inducible RNA binding protein (CIRP) expression is modulated by alternative mRNAs
    • Al-Fageeh, M. B. and Smales, C. M. (2009) Cold-inducible RNA binding protein (CIRP) expression is modulated by alternative mRNAs. RNA 15, 1164-1176
    • (2009) RNA , vol.15 , pp. 1164-1176
    • Al-Fageeh, M.B.1    Smales, C.M.2
  • 19
    • 79953204942 scopus 로고    scopus 로고
    • ATR (ataxia telangiectasia mutated-and Rad3-related kinase) is activated by mild hypothermia in mammalian cells and subsequently activates p53
    • Roobol, A., Roobol, J., Carden, M. J., Bastide, A., Willis, A. E., Dunn, W. B., Goodacre, R. and Smales, C. M. (2011) ATR (ataxia telangiectasia mutated-and Rad3-related kinase) is activated by mild hypothermia in mammalian cells and subsequently activates p53. Biochem. J. 435, 499-508
    • Biochem. J. , vol.435 , pp. 499-508
    • Roobol, A.1    Roobol, J.2    Carden, M.J.3    Bastide, A.4    Willis, A.E.5    Dunn, W.B.6    Goodacre, R.7    Smales, C.M.M.8
  • 20
    • 0001856130 scopus 로고    scopus 로고
    • The roles of the cytosolic chaperone, CCT, in normal eukaryotic cell growth
    • Oxford University Press, Oxford
    • Willison, K. R. and Grantham, J. (2001) The roles of the cytosolic chaperone, CCT, in normal eukaryotic cell growth. In Molecular Chaperones in the Cell (Lund, P., ed.), pp. 90-118, Oxford University Press, Oxford
    • (2001) Molecular Chaperones in the Cell (Lund, P., Ed.) , pp. 90-118
    • Willison, K.R.1    Grantham, J.2
  • 21
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • Yam, A. Y., Xia, Y., Lin, H.-T. J., Burlingame, A., Gerstein, M. and Frydman, J. (2008) Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat. Struct. Mol. Biol. 15, 1255-1262
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    Lin, H.-T.J.3    Burlingame, A.4    Gerstein, M.5    Frydman, J.6
  • 23
    • 20344385029 scopus 로고    scopus 로고
    • CCT chaperonin complex is required for the biogenesis of functional Plk1
    • Liu, X., Lin, C. Y., Lei, M., Yan, S., Zhou, T. and Erikson, R. L. (2005) CCT chaperonin complex is required for the biogenesis of functional Plk1. Mol. Cell. Biol. 25, 4993-5010
    • Mol. Cell. Biol. , vol.25 , pp. 4993-5010
    • Liu, X.1    Lin, C.Y.2    Lei, M.3    Yan, S.4    Zhou, T.5    Erikson, R.L.L.6
  • 24
    • 79961026866 scopus 로고    scopus 로고
    • The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins
    • Dekker, C., Roe, S. M., McCormack, E. A., Beuron, F., Pearl, L. H. and Willison, K. R. (2011) The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. EMBO J. 30, 3078-3090
    • (2011) EMBO J. , vol.30 , pp. 3078-3090
    • Dekker, C.1    Roe, S.M.2    McCormack, E.A.3    Beuron, F.4    Pearl, L.H.5    Willison, K.R.6
  • 25
    • 17844378217 scopus 로고    scopus 로고
    • Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by em analysis
    • Rivenzon-Segal, D., Wolf, S. G., Shimon, L., Willison, K. R. and Horovitz, A. (2005) Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat. Struct. Mol. Biol. 12, 233-237
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 233-237
    • Rivenzon-Segal, D.1    Wolf, S.G.2    Shimon, L.3    Willison, K.R.4    Horovitz, A.5
  • 28
    • 70349780560 scopus 로고    scopus 로고
    • The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries
    • Sha, Z., Brill, L. M., Cabrera, R., Kleifeld, O., Scheliga, J. S., Glickman, M. H., Chang, E. C. and Wolf, D. A. (2009) The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries. Mol. Cell 36, 141-152
    • (2009) Mol. Cell , vol.36 , pp. 141-152
    • Sha, Z.1    Brill, L.M.2    Cabrera, R.3    Kleifeld, O.4    Scheliga, J.S.5    Glickman, M.H.6    Chang, E.C.7    Wolf, D.A.8
  • 30
    • 0032587044 scopus 로고    scopus 로고
    • Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle
    • Roobol, A. and Carden, M. J. (1999) Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle. Eur. J. Cell Biol. 78, 21-32
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 21-32
    • Roobol, A.1    Carden, M.J.2
  • 31
    • 0035476376 scopus 로고    scopus 로고
    • Internal ribosome entry segment-mediated initiation of c-Myc protein synthesis following genotoxic stress
    • Subkhankulova, T., Mitchell, S. A. and Willis, A. E. (2001) Internal ribosome entry segment-mediated initiation of c-Myc protein synthesis following genotoxic stress. Biochem. J. 359, 183-192
    • (2001) Biochem. J. , vol.359 , pp. 183-192
    • Subkhankulova, T.1    Mitchell, S.A.2    Willis, A.E.3
  • 32
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma bruceiby a library of monoclonal antibodies
    • Woods, A., Sherwin, T., Sasse, R., MacRae, T. H., Baines, A. J. and Gull, K. (1989) Definition of individual components within the cytoskeleton of Trypanosoma bruceiby a library of monoclonal antibodies. J. Cell Sci. 93, 491-500
    • (1989) J. Cell Sci. , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    Macrae, T.H.4    Baines, A.J.5    Gull, K.6
  • 33
    • 0031916967 scopus 로고    scopus 로고
    • Mammalian cytosolic chaperonin
    • Cowan, N. J. (1998) Mammalian cytosolic chaperonin. Methods Enzymol. 290, 230-241
    • (1998) Methods Enzymol. , vol.290 , pp. 230-241
    • Cowan, N.J.1
  • 34
    • 33745272858 scopus 로고    scopus 로고
    • Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/γ subunit
    • Pappenberger, G., McCormack, E. A. and Willison, K. R. (2006) Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/γ subunit. J. Mol. Biol. 360, 484-496
    • (2006) J. Mol. Biol. , vol.360 , pp. 484-496
    • Pappenberger, G.1    McCormack, E.A.2    Willison, K.R.3
  • 35
    • 0034680592 scopus 로고    scopus 로고
    • Defining the eukaryotic cytosolic chaperonin-binding sites in human tubulins
    • Ritco-Vonsovici, M. and Willison, K. R. (2000) Defining the eukaryotic cytosolic chaperonin-binding sites in human tubulins. J. Mol. Biol. 304, 81-98
    • (2000) J. Mol. Biol. , vol.304 , pp. 81-98
    • Ritco-Vonsovici, M.1    Willison, K.R.2
  • 36
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev, A. and Wagner, G. (2004) Translation initiation: structures, mechanisms and evolution. Q. Rev. Biophys. 37, 197-284
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 37
    • 0345094935 scopus 로고    scopus 로고
    • Eukaryotic chaperonins: Lubricating the folding of WD-repeat proteins
    • Craig, E. A. (2003) Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins. Curr. Biol. 13, R904-R905
    • (2003) Curr. Biol. , vol.13
    • Craig, E.A.1
  • 38
    • 0343907201 scopus 로고    scopus 로고
    • Cytoplasmic chaperonin containing TCP-1: Structural and functional characterization
    • Melki, R., Batelier, G., Soulíe, S. and Williams, Jr, R. C. (1997) Cytoplasmic chaperonin containing TCP-1: structural and functional characterization. Biochemistry 36, 5817-5826
    • (1997) Biochemistry , vol.36 , pp. 5817-5826
    • Melki, R.1    Batelier, G.2    Soulíe, S.3    Williams Jr., R.C.4
  • 39
    • 57749102552 scopus 로고    scopus 로고
    • Substrate selection by the proteasome during degradation of protein complexes
    • Prakash, S., Inobe, T., Hatch, A. J. and Matouschek, A. (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat. Chem. Biol. 5, 29-36
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 29-36
    • Prakash, S.1    Inobe, T.2    Hatch, A.J.3    Matouschek, A.4
  • 40
    • 77449113481 scopus 로고    scopus 로고
    • Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly
    • Brackley, K. I. and Grantham, J. (2010) Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly. Exp. Cell Res. 316, 543-553
    • (2010) Exp. Cell Res. , vol.316 , pp. 543-553
    • Brackley, K.I.1    Grantham, J.2
  • 42
    • 0041669463 scopus 로고    scopus 로고
    • The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20
    • Camasses, A., Bogdanova, A., Shevchenko, A. and Zachariae, W. (2003) The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20. Mol. Cell 12, 87-100
    • (2003) Mol. Cell , vol.12 , pp. 87-100
    • Camasses, A.1    Bogdanova, A.2    Shevchenko, A.3    Zachariae, W.4
  • 43
    • 75149146624 scopus 로고    scopus 로고
    • The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways
    • Lee, J. P., Brauweiler, A., Rudolph, M., Hooper, J. E., Drabkin, H. A. and Gemmill, R. M. (2010) The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways. Mol. Cancer Res. 8, 93-106
    • Mol. Cancer Res. , vol.8 , pp. 93-106
    • Lee, J.P.1    Brauweiler, A.2    Rudolph, M.3    Hooper, J.E.4    Drabkin, H.A.5    Gemmill, R.M.M.6
  • 44
    • 84867302560 scopus 로고    scopus 로고
    • Cryptic transcripts from a ubiquitous plasmid origin of replication confound tests for cis-regulatory function
    • Lemp, N. A., Hiraoka, K., Kasahara, N. and Logg, C. R. (2012) Cryptic transcripts from a ubiquitous plasmid origin of replication confound tests for cis-regulatory function. Nucleic Acids Res. 40, 7280-7290
    • (2012) Nucleic Acids Res. , vol.40 , pp. 7280-7290
    • Lemp, N.A.1    Hiraoka, K.2    Kasahara, N.3    Logg, C.R.4
  • 45
    • 84874742066 scopus 로고    scopus 로고
    • Ribosomal protein S25 dependency reveals a common mechanism for diverse internal ribosome entry sites and ribosome shunting
    • Hertz, M. I., Landry, D. M., Willis, A. E., Luo, G. and Thompson, S. R. (2013) Ribosomal protein S25 dependency reveals a common mechanism for diverse internal ribosome entry sites and ribosome shunting. Mol. Cell. Biol. 33, 1016-1026
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 1016-1026
    • Hertz, M.I.1    Landry, D.M.2    Willis, A.E.3    Luo, G.4    Thompson, S.R.5
  • 46
    • 0037197962 scopus 로고    scopus 로고
    • Characterization of the c-MYC-regulated transcriptome by SAGE: Identification and analysis of c-MYC target genes
    • Menssen, A. and Hermeking, H. (2002) Characterization of the c-MYC-regulated transcriptome by SAGE: identification and analysis of c-MYC target genes. Proc. Natl. Acad. Sci. U.S.A. 99, 6274-6279
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6274-6279
    • Menssen, A.1    Hermeking, H.2
  • 47
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • Frydman, J., Erdjument-Bromage, H., Tempst, P. and Hartl, F. U. (1999) Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat. Struct. Biol. 6, 697-705
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Hartl, F.U.4
  • 49
    • 67649379040 scopus 로고    scopus 로고
    • P90 ribosomal S6 kinase and p70 S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin and nutrient signaling
    • Abe, Y., Yoon, S.-O., Kubota, K., Mendoza, M. C., S.P., G. and Blenis, J. (2009) p90 ribosomal S6 kinase and p70 S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin and nutrient signaling. J. Biol. Chem. 284, 14939-14948
    • (2009) J. Biol. Chem. , vol.284 , pp. 14939-14948
    • Abe, Y.1    Yoon, S.-O.2    Kubota, K.3    Mendoza, M.C.S.P.G.4    Blenis, J.5
  • 50
    • 79955847641 scopus 로고    scopus 로고
    • A phospho-proteomic screen identifies novel S6K1 and mTORC1 substrates revealing additional complexity in the signaling network regulating cell growth
    • Jastrzebski, K., Hannan, K. M., House, C. M., Hung, S. S. C., Pearson, R. B. and Hannan, R. D. (2011) A phospho-proteomic screen identifies novel S6K1 and mTORC1 substrates revealing additional complexity in the signaling network regulating cell growth. Cell. Signal. 23, 1338-1347
    • Cell. Signal. , vol.23 , pp. 1338-1347
    • Jastrzebski, K.1    Hannan, K.M.2    House, C.M.3    Hung, S.S.C.4    Pearson, R.B.5    Hannan, R.D.D.6
  • 51
    • 70350523886 scopus 로고    scopus 로고
    • Using microarray technology to select housekeeping genes in Chinese hamster ovary cells
    • Bahr, S. M., Borgschulte, T., Kayser, K. J. and Lin, N. (2009) Using microarray technology to select housekeeping genes in Chinese hamster ovary cells. Biotechnol. Bioeng. 104, 1041-1046
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 1041-1046
    • Bahr, S.M.1    Borgschulte, T.2    Kayser, K.J.3    Lin, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.