메뉴 건너뛰기




Volumn 409, Issue 1, 2008, Pages 223-231

The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2

Author keywords

ABC protein; CK2; eIF2; Ribosome; Translation initiation

Indexed keywords

POLYSOMAL FRACTIONS; RIBOSOME; TRANSLATION INITIATION;

EID: 38149006389     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070811     Document Type: Article
Times cited : (29)

References (18)
  • 1
    • 17144462873 scopus 로고    scopus 로고
    • ABC50, a novel human ATP-binding cassette protein found in tumor necrosis factor-α-stimulated synoviocytes
    • Richard, M., Drouin, R. and Beaulieu, A. D. (1998) ABC50, a novel human ATP-binding cassette protein found in tumor necrosis factor-α-stimulated synoviocytes. Genomics 53, 137-145
    • (1998) Genomics , vol.53 , pp. 137-145
    • Richard, M.1    Drouin, R.2    Beaulieu, A.D.3
  • 2
    • 0034602140 scopus 로고    scopus 로고
    • ABC50 interacts with eukaryotic initiation factor (eIF) 2 and binds to ribosomes in an ATP-dependent manner
    • Tyzack, J. K., Belsham, G. J., Wang, X. and Proud, C. G. (2000) ABC50 interacts with eukaryotic initiation factor (eIF) 2 and binds to ribosomes in an ATP-dependent manner. J. Biol. Chem. 275, 34131-34139
    • (2000) J. Biol. Chem , vol.275 , pp. 34131-34139
    • Tyzack, J.K.1    Belsham, G.J.2    Wang, X.3    Proud, C.G.4
  • 3
    • 0029001571 scopus 로고
    • GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2α kinase GCN2 in amino acid starved cells
    • Vazquez de Aldana, C. R., Marton, M. J. and Hinnebusch, A. G. (1995) GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2α kinase GCN2 in amino acid starved cells. EMBO J. 14, 3184-3189.
    • (1995) EMBO J , vol.14 , pp. 3184-3189
    • Vazquez de Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 4
    • 1842287951 scopus 로고    scopus 로고
    • Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2α kinase GCN2
    • Marton, M. J., Vazquez de Aldana, C. R., Qu, H., Chakraburtty, K. and Hinnebusch, A. G. (1997) Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2α kinase GCN2. Mol. Cell. Biol. 17, 4474-4489
    • (1997) Mol. Cell. Biol , vol.17 , pp. 4474-4489
    • Marton, M.J.1    Vazquez de Aldana, C.R.2    Qu, H.3    Chakraburtty, K.4    Hinnebusch, A.G.5
  • 5
    • 0035794125 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein
    • Das, S., Ghosh, R. and Maitra, U. (2001) Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein. J. Biol. Chem. 276, 6720-6726
    • (2001) J. Biol. Chem , vol.276 , pp. 6720-6726
    • Das, S.1    Ghosh, R.2    Maitra, U.3
  • 6
    • 0035191271 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein
    • Paulin, F. E. M., Campbell, L. E., O'Brien, K., Loughlin, A. J. and Proud, C. G. (2001) Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein. Curr. Biol. 11, 55-59
    • (2001) Curr. Biol , vol.11 , pp. 55-59
    • Paulin, F.E.M.1    Campbell, L.E.2    O'Brien, K.3    Loughlin, A.J.4    Proud, C.G.5
  • 7
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud, C. G. (2005) eIF2 and the control of cell physiology. Semin. Cell Dev. Biol. 16, 3-12
    • (2005) Semin. Cell Dev. Biol , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 8
    • 28844478867 scopus 로고    scopus 로고
    • eIF2B, a mediator of general and gene-specific translational control
    • Pavitt, G. D. (2005) eIF2B, a mediator of general and gene-specific translational control. Biochem. Soc. Trans. 33, 1487-1492
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1487-1492
    • Pavitt, G.D.1
  • 9
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano, K., Krishnamoorthy, T., Phan, L., Pavitt, G. D. and Hinnebusch, A. G. (1999) Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18, 1673-1688
    • (1999) EMBO J , vol.18 , pp. 1673-1688
    • Asano, K.1    Krishnamoorthy, T.2    Phan, L.3    Pavitt, G.D.4    Hinnebusch, A.G.5
  • 10
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano, K., Shalev, A., Phan, L., Nielsen, K., Clayton, J., Valassek, L., Donahue, T. F. and Hinnebusch, A. G. (2001) Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J. 20, 2326-2337
    • (2001) EMBO J , vol.20 , pp. 2326-2337
    • Asano, K.1    Shalev, A.2    Phan, L.3    Nielsen, K.4    Clayton, J.5    Valassek, L.6    Donahue, T.F.7    Hinnebusch, A.G.8
  • 11
    • 0035882047 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2B: Identification of multiple phosphorylation sites in the ε subunit and their roles in vivo
    • Wang, X., Paulin, F. E. M., Campbell, L. E., Gomez, E., O'Brien, K., Morrice, N. and Proud, C. G. (2001) Eukaryotic initiation factor 2B: identification of multiple phosphorylation sites in the ε subunit and their roles in vivo. EMBO J. 20, 4349-4359
    • (2001) EMBO J , vol.20 , pp. 4349-4359
    • Wang, X.1    Paulin, F.E.M.2    Campbell, L.E.3    Gomez, E.4    O'Brien, K.5    Morrice, N.6    Proud, C.G.7
  • 12
    • 27344436940 scopus 로고    scopus 로고
    • CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cycle progression
    • Homma, M. K., Wada, I., Suzuki, T., Yamaki, J., Krebs, E. G. and Homma, Y. (2005) CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cycle progression. Proc. Natl. Acad. Sci. U.S.A. 102, 15688-15693
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 15688-15693
    • Homma, M.K.1    Wada, I.2    Suzuki, T.3    Yamaki, J.4    Krebs, E.G.5    Homma, Y.6
  • 13
    • 0036493241 scopus 로고    scopus 로고
    • Phosphorylation of mammalian translation initiation factor 5 (eIF5) in vitro and in vivo
    • Majumdar, R., Bandyopadhyay, A., Deng, H. and Maitra, U. (2002) Phosphorylation of mammalian translation initiation factor 5 (eIF5) in vitro and in vivo. Nucleic Acids Res. 30, 1154-1162
    • (2002) Nucleic Acids Res , vol.30 , pp. 1154-1162
    • Majumdar, R.1    Bandyopadhyay, A.2    Deng, H.3    Maitra, U.4
  • 14
    • 0033581880 scopus 로고    scopus 로고
    • ATR is a caffeine-sensitive, DNA-activated protein kinase with a substrate specificity distinct from DNA-PK
    • Hall-Jackson, C. A., Cross, D. A., Morrice, N. and Smythe, C. (1999) ATR is a caffeine-sensitive, DNA-activated protein kinase with a substrate specificity distinct from DNA-PK. Oncogene 18, 6707-6713
    • (1999) Oncogene , vol.18 , pp. 6707-6713
    • Hall-Jackson, C.A.1    Cross, D.A.2    Morrice, N.3    Smythe, C.4
  • 15
    • 0026055806 scopus 로고
    • Purification of His-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies
    • Hoffmann, A. and Roeder, R. G. (1991) Purification of His-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies. Nucleic Acids Res. 19, 6337-6338
    • (1991) Nucleic Acids Res , vol.19 , pp. 6337-6338
    • Hoffmann, A.1    Roeder, R.G.2
  • 16
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
    • Boyle, W. J., Smeal, T., Defize, L. H., Angel, P., Woodgett, J. R., Karin, M. and Hunter, T. (1991) Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell 64, 573-584
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.3    Angel, P.4    Woodgett, J.R.5    Karin, M.6    Hunter, T.7
  • 17
    • 33644674733 scopus 로고    scopus 로고
    • Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer
    • Williamson, B. L., Marchese, J. and Morrice, N. A. (2006) Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer. Mol. Cell Proteomics. 5, 337-346
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 337-346
    • Williamson, B.L.1    Marchese, J.2    Morrice, N.A.3
  • 18
    • 9644291558 scopus 로고    scopus 로고
    • Physical association of eukaryotic initiation factor (eIF) 5 carboxyl-terminal domain with the lysine-rich eIF2β segment strongly enhances its binding to eIF3
    • Singh, C. R., Yamamoto, Y. and Asano, K. (2004) Physical association of eukaryotic initiation factor (eIF) 5 carboxyl-terminal domain with the lysine-rich eIF2β segment strongly enhances its binding to eIF3. J. Biol. Chem. 279, 49644-49655
    • (2004) J. Biol. Chem , vol.279 , pp. 49644-49655
    • Singh, C.R.1    Yamamoto, Y.2    Asano, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.