메뉴 건너뛰기




Volumn 283, Issue 2, 2003, Pages 237-246

Negative regulation of the protection of eIF2α phosphorylation activity by a unique acidic domain present at the N-terminus of p67

Author keywords

eIF2 phosphorylation; KRC 7 cells; p67; p67 deglycosylase; POEP activity

Indexed keywords

ALANINE; AMINO ACID; INITIATION FACTOR 2; MUTANT PROTEIN; PROTEIN; PROTEIN P67; UNCLASSIFIED DRUG;

EID: 0037442848     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(02)00042-3     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey J.W.B. Translational control in mammalian cells. Annu. Rev. Biochem. 60:1991;717-755.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 2
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratories Press
    • Merrick W.C., Hershey J.W.B. Pathway and mechanism of initiation of protein synthesis. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational Control in Gene Expression. 2000;33-88 Cold Spring Harbor Laboratories Press, Cold Spring Harbor, NY.
    • (2000) Translational Control in Gene Expression , pp. 33-88
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 3
    • 0033527640 scopus 로고    scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine, or tyrosine at residue 51 in eukaryotic initiation factor 2α
    • Lu J., O'Hara E.B., Trieslmann B.A., Romano P.R., Dever T.E. The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine, or tyrosine at residue 51 in eukaryotic initiation factor 2α J. Biol. Chem. 274:1999;32198-32203.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32198-32203
    • Lu, J.1    O'Hara, E.B.2    Trieslmann, B.A.3    Romano, P.R.4    Dever, T.E.5
  • 4
    • 0028171125 scopus 로고
    • EIF-2 kinases, regulators of general and gene-specific translation initiation
    • Wek R.C. eIF-2 kinases, regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19:1994;491-496.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 5
    • 0002470681 scopus 로고    scopus 로고
    • Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratories Press
    • Hinnebusch A.G. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational Control in Gene Expression. 2000;185-244 Cold Spring Harbor Laboratories Press, Cold Spring Harbor, NY.
    • (2000) Translational Control in Gene Expression , pp. 185-244
    • Hinnebusch, A.G.1
  • 6
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever T.E. Gene-specific regulation by general translation factors. Cell. 108:2002;545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 7
    • 0001815885 scopus 로고    scopus 로고
    • Double-stranded RNA-activated protein kinase, PKR
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratories Press
    • Kaufman R.J. Double-stranded RNA-activated protein kinase, PKR. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational control in Gene Expression. 2000;503-528 Cold Spring Harbor Laboratories Press, Cold Spring Harbor, NY.
    • (2000) Translational control in Gene Expression , pp. 503-528
    • Kaufman, R.J.1
  • 8
    • 0001657903 scopus 로고    scopus 로고
    • Heme-regulated eIF2α kinase
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratories Press
    • Chen J.J. Heme-regulated eIF2α kinase. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational Control in Gene Expression. 2000;529-546 Cold Spring Harbor Laboratories Press, Cold Spring Harbor, NY.
    • (2000) Translational Control in Gene Expression , pp. 529-546
    • Chen, J.J.1
  • 9
    • 0003113283 scopus 로고    scopus 로고
    • PERK and translational control by stress in the endoplasmic reticulum
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratories Press
    • Ron D., Harding H.P. PERK and translational control by stress in the endoplasmic reticulum. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational Control in Gene Expression. 2000;547-560 Cold Spring Harbor Laboratories Press, Cold Spring Harbor, NY.
    • (2000) Translational Control in Gene Expression , pp. 547-560
    • Ron, D.1    Harding, H.P.2
  • 10
    • 0003159477 scopus 로고    scopus 로고
    • Translational reprogramming during influenza virus infection
    • J.W.B. Hershey, M.B. Mathews, & N. Sonenberg. Cold Spring Harbor, NY: Cold Spring Harbor Laboratories Press
    • Tan S.L., Gale M. Jr., Katze M.G. Translational reprogramming during influenza virus infection. Hershey J.W.B., Mathews M.B., Sonenberg N. Translational control in gene expression. 2000;933-950 Cold Spring Harbor Laboratories Press, Cold Spring Harbor, NY.
    • (2000) Translational control in gene expression , pp. 933-950
    • Tan, S.L.1    Gale M., Jr.2    Katze, M.G.3
  • 11
    • 0028008882 scopus 로고
    • Molecular mechanisms in the control of translation by hormones and growth factors
    • Redpath N.T., Proud C.G. Molecular mechanisms in the control of translation by hormones and growth factors. Biochim. Biophy. Acta. 1220:1994;147-162.
    • (1994) Biochim. Biophy. Acta , vol.1220 , pp. 147-162
    • Redpath, N.T.1    Proud, C.G.2
  • 12
    • 0034144404 scopus 로고    scopus 로고
    • MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms
    • Datta B. MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms. Biochimic. 82:2000;95-107.
    • (2000) Biochimic , vol.82 , pp. 95-107
    • Datta, B.1
  • 13
    • 0035213737 scopus 로고    scopus 로고
    • Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67
    • Datta R., Choudhury P., Bhattacharya M., Leon F.S., Zhou Y., Datta B. Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67. Biochimie. 83:2001;919-931.
    • (2001) Biochimie , vol.83 , pp. 919-931
    • Datta, R.1    Choudhury, P.2    Bhattacharya, M.3    Leon, F.S.4    Zhou, Y.5    Datta, B.6
  • 16
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine amino peptidase from Escherichia coli: A new type of proteolytic enzyme
    • Roderick S.L., Matthews B.W. Structure of the cobalt-dependent methionine amino peptidase from Escherichia coli a new type of proteolytic enzyme . Biochemistry. 32:1993;3907-3912.
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 17
    • 0028198617 scopus 로고
    • Sequence and structure comparison suggest that methionine amino peptidase, prolidase, amino peptidase P, and creatinase share a common fold
    • Bazan J.F., Weaver L.H., Roderick S.L., Huber R., Matthews B.W. Sequence and structure comparison suggest that methionine amino peptidase, prolidase, amino peptidase P, and creatinase share a common fold. Proc. Natl.Acad. Sci. USA. 91:1993;2473-2477.
    • (1993) Proc. Natl.Acad. Sci. USA , vol.91 , pp. 2473-2477
    • Bazan, J.F.1    Weaver, L.H.2    Roderick, S.L.3    Huber, R.4    Matthews, B.W.5
  • 18
    • 0032976823 scopus 로고    scopus 로고
    • Methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in Drosophila
    • Cutforth T., Gaul U.A. Methionine aminopeptidase and putative regulator of translation initiation is required for cell growth and patterning in Drosophila. Mechanisms Dev. 82:1999;23-28.
    • (1999) Mechanisms Dev. , vol.82 , pp. 23-28
    • Cutforth, T.1    Gaul, U.A.2
  • 19
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li X., Chang Y.H. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl. Acad. Sci. USA. 92:1995;2357-12361.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2357-12361
    • Li, X.1    Chang, Y.H.2
  • 21
    • 0030204204 scopus 로고    scopus 로고
    • Methionine aminopeptidase-1: The MAP of the mitochondrion?
    • Keeling P.J., Doolittle W.F. Methionine aminopeptidase-1 the MAP of the mitochondrion? Trends Biochem. Sci. 21:1996;285-286.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 285-286
    • Keeling, P.J.1    Doolittle, W.F.2
  • 23
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu S., Widom J., Kemp C.W., Crews C.M., Clardy J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science. 282:1998;1324-1327.
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 24
    • 13044300888 scopus 로고    scopus 로고
    • Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2
    • Griffith E.C., Su Z., Niwayama S., Ramsay C.A., Chang Y.-W., Wu Z., Liu J.O. Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2. Proc. Natl. Acad. Sci. USA. 95:1997;15183-15188.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15183-15188
    • Griffith, E.C.1    Su, Z.2    Niwayama, S.3    Ramsay, C.A.4    Chang, Y.-W.5    Wu, Z.6    Liu, J.O.7
  • 25
    • 0031171961 scopus 로고    scopus 로고
    • Methionine aminopeptidase (type 2) is the common target for angiogenesis inihibitors AGM-14470 and ovalicin
    • Griffith E.C., Su Z., Turk B.E., Chen S., Chang Y.-W., Wu Z., Biemann K., Liu J.O. Methionine aminopeptidase (type 2) is the common target for angiogenesis inihibitors AGM-14470 and ovalicin. Chem. Biol. 4:1997;461-471.
    • (1997) Chem. Biol. , vol.4 , pp. 461-471
    • Griffith, E.C.1    Su, Z.2    Turk, B.E.3    Chen, S.4    Chang, Y.-W.5    Wu, Z.6    Biemann, K.7    Liu, J.O.8
  • 26
    • 0034054364 scopus 로고    scopus 로고
    • Selective inhibition of endothelial cell proliferation by fumagillin is not due to differential expression of methionine aminopeptidases
    • Wang J., Lou P., Henkin J. Selective inhibition of endothelial cell proliferation by fumagillin is not due to differential expression of methionine aminopeptidases. J. Cell. Biochem. 77:2000;465-473.
    • (2000) J. Cell. Biochem. , vol.77 , pp. 465-473
    • Wang, J.1    Lou, P.2    Henkin, J.3
  • 30
    • 0033080447 scopus 로고    scopus 로고
    • Induction of apoptosis due to lowering the level of eukaryotic initiation factor 2-associated protein, p67, from mammalian cells by antisense approach
    • Datta B., Datta R. Induction of apoptosis due to lowering the level of eukaryotic initiation factor 2-associated protein, p67, from mammalian cells by antisense approach. Exp. Cell Res. 246:1999;376-383.
    • (1999) Exp. Cell Res. , vol.246 , pp. 376-383
    • Datta, B.1    Datta, R.2
  • 31
    • 0033542738 scopus 로고    scopus 로고
    • 2/M boundary in human osteosarcoma cells correlates with deglycosylation of p67 and a decreased rate of protein synthesis
    • 2/M boundary in human osteosarcoma cells correlates with deglycosylation of p67 and a decreased rate of protein synthesis. Exp. Cell Res. 250:1999;223-230.
    • (1999) Exp. Cell Res. , vol.250 , pp. 223-230
    • Datta, B.1    Datta, R.2    Mukherjee, S.3    Zhang, Z.4
  • 32
    • 0029861053 scopus 로고    scopus 로고
    • P202, an interferon-inducible modulator of transcription, inhibits transcriptional activation by the p53 tumor suppressor protein, and a segment from the p53-binding protein 1 that binds to p202 overcomes this inhibition
    • Datta B., Li B., Choubey D., Nallur G., Lengyel P. p202, an interferon-inducible modulator of transcription, inhibits transcriptional activation by the p53 tumor suppressor protein, and a segment from the p53-binding protein 1 that binds to p202 overcomes this inhibition. J. Biol. Chem. 271:1998;27544-27555.
    • (1998) J. Biol. Chem. , vol.271 , pp. 27544-27555
    • Datta, B.1    Li, B.2    Choubey, D.3    Nallur, G.4    Lengyel, P.5
  • 33
    • 0012332645 scopus 로고
    • Roles of a 67 kDa polypeptide in protein synthesis inhibition in heme-deficient reticulocyte lysates
    • Datta B., Chakrabarti D., Roy A.L., Gupta N.K. Roles of a 67 kDa polypeptide in protein synthesis inhibition in heme-deficient reticulocyte lysates. Proc. Natl. Acad. Sci. USA. 85:1988;3324-3328.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3324-3328
    • Datta, B.1    Chakrabarti, D.2    Roy, A.L.3    Gupta, N.K.4
  • 34
    • 0026783641 scopus 로고
    • Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae
    • Chang Y.H., Teicher U., Smith J.A. Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae. J. Biol. Chem. 267:1992;8007-8011.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8007-8011
    • Chang, Y.H.1    Teicher, U.2    Smith, J.A.3
  • 35
    • 0026703067 scopus 로고
    • Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins
    • Kendall R.L., Bradshaw R.A. Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins. J. Biol. Chem. 267:1992;20667-20673.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20667-20673
    • Kendall, R.L.1    Bradshaw, R.A.2
  • 36
    • 0031573467 scopus 로고    scopus 로고
    • A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2
    • Klinkenberg M., Ling C., Chang Y.-H. A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2. Arch. Biochem. Biophys. 347:1997;193-200.
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 193-200
    • Klinkenberg, M.1    Ling, C.2    Chang, Y.-H.3
  • 37
    • 0028819132 scopus 로고
    • Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae is important for normal growth
    • Zuo S., Guo Q., Ling C., Chang Y.-H. Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae is important for normal growth. Mol. Gen. Genet. 246:1995;247-253.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 247-253
    • Zuo, S.1    Guo, Q.2    Ling, C.3    Chang, Y.-H.4
  • 38
    • 0034720794 scopus 로고    scopus 로고
    • In vivo regulation of protein synthesis by phosphorylation of the α subunit of wheat eukaryotic initiation factor 2
    • Gil J., Esteban M., Roth D. In vivo regulation of protein synthesis by phosphorylation of the α subunit of wheat eukaryotic initiation factor 2. Biochemistry. 39:2000;7521-7530.
    • (2000) Biochemistry , vol.39 , pp. 7521-7530
    • Gil, J.1    Esteban, M.2    Roth, D.3
  • 39
    • 0032052990 scopus 로고    scopus 로고
    • Expression and purification of the α-subunit of eukaryotic initiation factor eIF2: Use as a kinase substrate
    • Kimball S.R., Horetsky R.L., Jagus R., Jefferson L.S. Expression and purification of the α-subunit of eukaryotic initiation factor eIF2 use as a kinase substrate . Protein Expression Purif. 12:1998;415-419.
    • (1998) Protein Expression Purif. , vol.12 , pp. 415-419
    • Kimball, S.R.1    Horetsky, R.L.2    Jagus, R.3    Jefferson, L.S.4
  • 40
    • 0032930054 scopus 로고    scopus 로고
    • Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18
    • Kumar K.U., Srivastava S.R., Kaufman R.J. Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18. Mol. Cell Biol. 19:1999;1116-1125.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1116-1125
    • Kumar, K.U.1    Srivastava, S.R.2    Kaufman, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.