메뉴 건너뛰기




Volumn 39, Issue 19, 2011, Pages 8314-8328

Mechanisms of translational regulation by a human eIF5-mimic protein

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 2B EPSILON; INITIATION FACTOR 3; INITIATION FACTOR 5; TRANSLATION FACTOR EIF5 MIMIC PROTEIN 1; UNCLASSIFIED DRUG;

EID: 80455149675     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr339     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds Cold Spring Harbor Lab Press, Cold Spring Harbor, NY
    • Pestova, T.V., Lorsch, J.R. and Hellen, C.U.T. (2007) The mechanism of translation initiation in eukaryotes. In Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds), Translational Control in Biology and Medicine. Cold Spring Harbor Lab Press, Cold Spring Harbor, NY, pp. 87-128.
    • (2007) Translational Control in Biology and Medicine , pp. 87-128
    • Pestova, T.V.1    Lorsch, J.R.2    Hellen, C.U.T.3
  • 2
    • 34249665243 scopus 로고    scopus 로고
    • Mechanism of translation initiation in the yeast Saccharomyces cerevisiae
    • Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds Cold Spring Harbor Lab Press, Cold Spring Harbor, NY
    • Hinnebusch, A.G., Dever, T.E. and Asano, K. (2007) Mechanism of translation initiation in the yeast Saccharomyces cerevisiae. In Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds), Translational Control in Biology and Medicine. Cold Spring Harbor Lab Press, Cold Spring Harbor, NY, pp. 225-268.
    • (2007) Translational Control in Biology and Medicine , pp. 225-268
    • Hinnebusch, A.G.1    Dever, T.E.2    Asano, K.3
  • 3
    • 33749340583 scopus 로고    scopus 로고
    • An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
    • Singh, C.R., Lee, B., Udagawa, T., Mohammad-Qureshi, S.S., Yamamoto, Y., Pavitt, G.D. and Asano, K. (2006) An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J., 25, 4537-4546.
    • (2006) EMBO J. , vol.25 , pp. 4537-4546
    • Singh, C.R.1    Lee, B.2    Udagawa, T.3    Mohammad-Qureshi, S.S.4    Yamamoto, Y.5    Pavitt, G.D.6    Asano, K.7
  • 4
    • 77952734403 scopus 로고    scopus 로고
    • EIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
    • Jennings, M.D. and Pavitt, G.D. (2010) eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation. Nature, 465, 378-381.
    • (2010) Nature , vol.465 , pp. 378-381
    • Jennings, M.D.1    Pavitt, G.D.2
  • 7
    • 36749050097 scopus 로고    scopus 로고
    • Signaling to translation initiation
    • Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds) Cold Spring Harbor Lab Press, Cold Spring Harbor, NY
    • Raught, B. and Gigras, A.-C. (2007) Signaling to Translation Initiation. In Mathews, M.B., Sonenberg, N. and and Hershey, J.W.B. (eds), Translational Control in Biology and Medicine. Cold Spring Harbor Lab Press, Cold Spring Harbor, NY, pp. 369-400.
    • (2007) Translational Control in Biology and Medicine , pp. 369-400
    • Raught, B.1    Gigras, A.-C.2
  • 8
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Be, 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 eIF2Be, 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
  • 9
    • 28044445673 scopus 로고    scopus 로고
    • The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3 and eIF4G
    • Yamamoto, Y., Singh, C.R., Marintchev, A., Hall, N.S., Hannig, E.M., Wagner, G. and Asano, K. (2005) The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3 and eIF4G. Proc. Natl Acad. Sci. USA, 102, 16164-16169.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16164-16169
    • Yamamoto, Y.1    Singh, C.R.2    Marintchev, A.3    Hall, N.S.4    Hannig, E.M.5    Wagner, G.6    Asano, K.7
  • 10
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation
    • Gomez, E., Mohammad, S.S. and Pavitt, G.P. (2002) Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation. EMBO J., 21, 5292-5301.
    • (2002) EMBO J. , vol.21 , pp. 5292-5301
    • Gomez, E.1    Mohammad, S.S.2    Pavitt, G.P.3
  • 11
    • 0034307347 scopus 로고    scopus 로고
    • A multifactor complex of eukaryotic initiation factors eIF1, eIF2, eIF3, eIF5, and initiator tRNAMet is an important translation initiation intermediate in vivo
    • Asano, K., Clayton, J., Shalev, A. and Hinnebusch, A.G. (2000) A multifactor complex of eukaryotic initiation factors eIF1, eIF2, eIF3, eIF5, and initiator tRNAMet is an important translation initiation intermediate in vivo. Genes Dev., 14, 2534-2546.
    • (2000) Genes Dev. , vol.14 , pp. 2534-2546
    • Asano, K.1    Clayton, J.2    Shalev, A.3    Hinnebusch, A.G.4
  • 12
    • 0031039645 scopus 로고    scopus 로고
    • A new translational regulator with homology to eukaryotic translation initiation factor 4G
    • Imataka, H., Olsen, S. and Sonenberg, N. (1997) A new translational regulator with homology to eukaryotic translation initiation factor 4G. EMBO J., 16, 817-825.
    • (1997) EMBO J. , vol.16 , pp. 817-825
    • Imataka, H.1    Olsen, S.2    Sonenberg, N.3
  • 14
    • 33748354044 scopus 로고    scopus 로고
    • P97/DAP5 is a ribosome-associated factor that facilitates protein synthesis and cell proliferation by modulating the synthesis of cell cylce proteins
    • Lee, S.H. and McCormick, F. (2006) p97/DAP5 is a ribosome-associated factor that facilitates protein synthesis and cell proliferation by modulating the synthesis of cell cylce proteins. EMBO J., 25, 4008-4019.
    • (2006) EMBO J. , vol.25 , pp. 4008-4019
    • Lee, S.H.1    McCormick, F.2
  • 16
    • 24944572189 scopus 로고    scopus 로고
    • EIF4G and CBP80 share a common origin and similar domain organization: Implications for the structure and function of eIF4G
    • Marintchev, A. and Wagner, G. (2005) eIF4G and CBP80 share a common origin and similar domain organization: Implications for the structure and function of eIF4G. Biochemistry, 44, 12265-12272.
    • (2005) Biochemistry , vol.44 , pp. 12265-12272
    • Marintchev, A.1    Wagner, G.2
  • 17
    • 0035807056 scopus 로고    scopus 로고
    • Purification and functional analysis of a novel leucine-zipper/ nucleotide-fold protein, BZAP45, stimulating cell cycle regulated histone H4 gene transcription
    • Mitra, P., Vaughan, P.S., Stein, J.L., Stein, G.S. and van Wijnen, A.J. (2001) Purification and functional analysis of a novel leucine-zipper/ nucleotide-fold protein, BZAP45, stimulating cell cycle regulated histone H4 gene transcription. Biochemistry, 40, 10693-10699.
    • (2001) Biochemistry , vol.40 , pp. 10693-10699
    • Mitra, P.1    Vaughan, P.S.2    Stein, J.L.3    Stein, G.S.4    Van Wijnen, A.J.5
  • 18
    • 0034714469 scopus 로고    scopus 로고
    • A visual intracellular classification strategy for uncharacterized human proteins
    • Hoya, M.R., Wahlestedt, C. and Höög, C. (2000) A visual intracellular classification strategy for uncharacterized human proteins. Exp. Cell Res., 259, 239-246.
    • (2000) Exp. Cell Res. , vol.259 , pp. 239-246
    • Hoya, M.R.1    Wahlestedt, C.2    Höög, C.3
  • 19
    • 34249049622 scopus 로고    scopus 로고
    • The F-actin-microtubule crosslinker Shot is a platform for Krasavietz-mediated translational regulation of midline axon repulsion
    • Lee, S., Nahm, M., Lee, M., Kwon, M., Kim, E., Zadeh, A.D., Cao, H., Kim, H.-J., Lee, Z.E., Oh, S.B. et al. (2007) The F-actin-microtubule crosslinker Shot is a platform for Krasavietz-mediated translational regulation of midline axon repulsion. Development, 134, 1767-1777.
    • (2007) Development , vol.134 , pp. 1767-1777
    • Lee, S.1    Nahm, M.2    Lee, M.3    Kwon, M.4    Kim, E.5    Zadeh, A.D.6    Cao, H.7    Kim, H.-J.8    Lee, Z.E.9    Oh, S.B.10
  • 21
    • 34249699125 scopus 로고    scopus 로고
    • Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo
    • Singh, C.R., Udagawa, T., Lee, B., Wassink, S., He, H., Yamamoto, Y., Anderson, J.T., Pavitt, G.D. and Asano, K. (2007) Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo. J. Mol. Biol., 370, 315-330.
    • (2007) J. Mol. Biol. , vol.370 , pp. 315-330
    • Singh, C.R.1    Udagawa, T.2    Lee, B.3    Wassink, S.4    He, H.5    Yamamoto, Y.6    Anderson, J.T.7    Pavitt, G.D.8    Asano, K.9
  • 22
    • 38449120943 scopus 로고    scopus 로고
    • Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, subcomplexes, and fragments from Saccharomyces cerevisiae
    • Mohammad-Qureshi, S.S., Haddad, R., Palmer, K.S., Richardson, J.P. and Pavitt, G.D. (2007) Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, subcomplexes, and fragments from Saccharomyces cerevisiae. Methods Enzymol., 431, 1-13.
    • (2007) Methods Enzymol. , vol.431 , pp. 1-13
    • Mohammad-Qureshi, S.S.1    Haddad, R.2    Palmer, K.S.3    Richardson, J.P.4    Pavitt, G.D.5
  • 23
    • 27344436940 scopus 로고    scopus 로고
    • CK2 phosphorylation of eukaryotic translation initiation factor 5 potentiates cell cylce 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 cylce progression. Proc. Natl Acad. Sci. USA, 102, 15688-15693.
    • (2005) Proc. Natl Acad. Sci. USA , 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
  • 24
    • 38449119672 scopus 로고    scopus 로고
    • Localization and characterization of protein-protein interaction sites
    • Singh, C.R. and Asano, K. (2007) Localization and characterization of protein-protein interaction sites. Methods Enzymol., 429, 139-161.
    • (2007) Methods Enzymol. , vol.429 , pp. 139-161
    • Singh, C.R.1    Asano, K.2
  • 26
    • 79251517391 scopus 로고    scopus 로고
    • Methods for analyzing eIF2 kinases and translational control in the unfolded protein response
    • Teske, B.F., Baird, T.D. and Wek, R.C. (2011) Methods for analyzing eIF2 kinases and translational control in the unfolded protein response. Methods Enzymol., 493, 333-356.
    • (2011) Methods Enzymol. , vol.493 , pp. 333-356
    • Teske, B.F.1    Baird, T.D.2    Wek, R.C.3
  • 27
    • 0034122792 scopus 로고    scopus 로고
    • Mutational analysis of mammalian translation initiation factor 5 (eIF5): Role of interaction between the beta subunit of eIF2 and eIF5 in eIF5 function in vitro and in vivo
    • Das, S. and Maitra, U. (2000) Mutational analysis of mammalian translation initiation factor 5 (eIF5): role of interaction between the beta subunit of eIF2 and eIF5 in eIF5 function in vitro and in vivo. Mol. Cell. Biol., 20, 3942-3950.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3942-3950
    • Das, S.1    Maitra, U.2
  • 28
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem, K.M. and Wek, R.C. (2004) Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl Acad. Sci. USA, 101, 11269-11274.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 29
    • 72149105341 scopus 로고    scopus 로고
    • The ELAV protein HuD stimulates cap-dependent translation in a poly(A)-and eIF4A-dependent manner
    • Fukao, A., Sasano, Y., Imataka, H., Inoue, K., Sakamoto, H., Sonenberg, N., Thoma, C. and Fujiwara, T. (2009) The ELAV protein HuD stimulates cap-dependent translation in a poly(A)-and eIF4A-dependent manner. Mol. Cell, 36, 1007-1017.
    • (2009) Mol. Cell , vol.36 , pp. 1007-1017
    • Fukao, A.1    Sasano, Y.2    Imataka, H.3    Inoue, K.4    Sakamoto, H.5    Sonenberg, N.6    Thoma, C.7    Fujiwara, T.8
  • 30
    • 33645677012 scopus 로고    scopus 로고
    • Structure of the eukaryotic initiation factor 5 reveals a fold common to several translation factors
    • Conte, M.R., Kelly, G., Babon, J., Sanfelice, D., youell, J., Smerdon, S.J. and Proud, C.G. (2006) Structure of the eukaryotic initiation factor 5 reveals a fold common to several translation factors. Biochemistry, 45, 4550-4558.
    • (2006) Biochemistry , vol.45 , pp. 4550-4558
    • Conte, M.R.1    Kelly, G.2    Babon, J.3    Sanfelice, D.4    Youell, J.5    Smerdon, S.J.6    Proud, C.G.7
  • 31
    • 35348989809 scopus 로고    scopus 로고
    • Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies
    • Hoyle, N.P., Castelli, L.M., Campbell, S.G., Holmes, L.E. and Ashe, M.P. (2007) Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies. J. Cell Biol., 179, 65-74.
    • (2007) J. Cell Biol. , vol.179 , pp. 65-74
    • Hoyle, N.P.1    Castelli, L.M.2    Campbell, S.G.3    Holmes, L.E.4    Ashe, M.P.5
  • 32
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • Buchan, J.R., Muhlrad, D. and Parker, R. (2008) P bodies promote stress granule assembly in Saccharomyces cerevisiae. J. Cell Biol., 183, 441-455.
    • (2008) J. Cell Biol. , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 33
    • 68949172267 scopus 로고    scopus 로고
    • Robust heat shock induces eIF2alphaphosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae
    • Grousl, T., Ivanov, P., Frýdlová, I., Vasicová, P., Janda, F., Vojtová, J., Maĺnská, K., Malcová, I., Nováková, L., Janosková, D. et al. (2009) Robust heat shock induces eIF2alphaphosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae. J. Cell Sci., 122, 2078-2088.
    • (2009) J. Cell Sci. , vol.122 , pp. 2078-2088
    • Grousl, T.1    Ivanov, P.2    Frýdlová, I.3    Vasicová, P.4    Janda, F.5    Vojtová, J.6    Malnská, K.7    Malcová, I.8    Nováková, L.9    Janosková, D.10
  • 34
    • 24944495906 scopus 로고    scopus 로고
    • Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: Implications for translational control
    • Campbell, S.G., Hoyle, N.P. and Ashe, M.P. (2005) Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: implications for translational control. J. Cell Biol., 170, 925-934.
    • (2005) J. Cell Biol. , vol.170 , pp. 925-934
    • Campbell, S.G.1    Hoyle, N.P.2    Ashe, M.P.3
  • 36
    • 0034024628 scopus 로고    scopus 로고
    • Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2b) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation
    • Gomez, E. and Pavitt, G.D. (2000) Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2b) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation. Mol. Cell Biol., 20, 3965-3976.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 3965-3976
    • Gomez, E.1    Pavitt, G.D.2
  • 37
    • 33846686409 scopus 로고    scopus 로고
    • Excitatory local circuits and their implications for alfactory processing in the fly antennal lobe
    • Shang, Y., Claridge-Chang, A., Sjulson, L., Pypaert, M. and Miesenbock, G.M. (2007) Excitatory local circuits and their implications for alfactory processing in the fly antennal lobe. Cell, 128, 601-612.
    • (2007) Cell , vol.128 , pp. 601-612
    • Shang, Y.1    Claridge-Chang, A.2    Sjulson, L.3    Pypaert, M.4    Miesenbock, G.M.5
  • 39
    • 0032489515 scopus 로고    scopus 로고
    • Trysine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich Syndome protein to PSTPIP, a cytoskeletal-associated protein
    • Wu, Y., Spencer, S.D. and Lasky, L.A. (1999) Trysine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich Syndome protein to PSTPIP, a cytoskeletal-associated protein. J. Biol. Chem., 273, 5765-5770.
    • (1999) J. Biol. Chem. , vol.273 , pp. 5765-5770
    • Wu, Y.1    Spencer, S.D.2    Lasky, L.A.3
  • 41
    • 34250354450 scopus 로고    scopus 로고
    • Mammalian tumor suppressor Int6 specifically targets hypoxia inducible factor 2alpha for degradation by hopoxia-and pVHL-independent regulation
    • Chen, L., Uchida, K., Endler, A. and Shibasaki, F. (2007) Mammalian tumor suppressor Int6 specifically targets hypoxia inducible factor 2alpha for degradation by hopoxia-and pVHL-independent regulation. J. Biol. Chem., 282, 12707-12716.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12707-12716
    • Chen, L.1    Uchida, K.2    Endler, A.3    Shibasaki, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.