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Volumn 15, Issue 7, 2014, Pages 11523-11538

Phosphorylation stoichiometries of human Eukaryotic initiation factors

Author keywords

Eukaryotic initiation factor; Mass spectrometry; Phosphorylation quantification; Translation

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 3; INITIATION FACTOR 4G; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN KINASE C ALPHA; ZINC BINDING PROTEIN;

EID: 84903432949     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms150711523     Document Type: Article
Times cited : (14)

References (45)
  • 2
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: New insights and challenges
    • doi:10.1101/cshperspect.a011544
    • Hinnebusch, A.G.; Lorsch, J.R. The mechanism of eukaryotic translation initiation: New insights and challenges. Cold Spring Harb. Perspect. Biol. 2012, 4, doi:10.1101/cshperspect.a011544.
    • (2012) Cold Spring Harb. Perspect. Biol , vol.4
    • Hinnebusch, A.G.1    Lorsch, J.R.2
  • 3
    • 78149243061 scopus 로고    scopus 로고
    • The molecular basis of translational control
    • Fraser, C.S. The molecular basis of translational control. Prog. Mol. Biol. Transl. Sci. 2009, 90, 1-51.
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.90 , pp. 1-51
    • Fraser, C.S.1
  • 4
    • 6344291066 scopus 로고    scopus 로고
    • Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection
    • Valasek, L.; Nielsen, K.H.; Zhang, F.; Fekete, C.A.; Hinnebusch, A.G. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol. Cell. Biol. 2004, 24, 9437-9455.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9437-9455
    • Valasek, L.1    Nielsen, K.H.2    Zhang, F.3    Fekete, C.A.4    Hinnebusch, A.G.5
  • 5
    • 33748924333 scopus 로고    scopus 로고
    • eIF3: A versatile scaffold for translation initiation complexes
    • Hinnebusch, A.G. eIF3: A versatile scaffold for translation initiation complexes. Trends Biochem. Sci. 2006, 31, 553-562.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 553-562
    • Hinnebusch, A.G.1
  • 6
    • 32044467711 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast
    • Jivotovskaya, A.V.; Valasek, L.; Hinnebusch, A.G.; Nielsen, K.H. Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast. Mol. Cell. Biol. 2006, 26, 1355-1372.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valasek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 7
    • 34250357112 scopus 로고    scopus 로고
    • eIF3j is located in the decoding center of the human 40S ribosomal subunit
    • Fraser, C.S.; Berry, K.E.; Hershey, J.W.; Doudna, J.A. eIF3j is located in the decoding center of the human 40S ribosomal subunit. Mol. Cell 2007, 26, 811-819.
    • (2007) Mol. Cell , vol.26 , pp. 811-819
    • Fraser, C.S.1    Berry, K.E.2    Hershey, J.W.3    Doudna, J.A.4
  • 8
    • 1542305510 scopus 로고    scopus 로고
    • The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro
    • Fraser, C.S.; Lee, J.Y.; Mayeur, G.L.; Bushell, M.; Doudna, J.A.; Hershey, J.W. The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro. J. Biol. Chem. 2004, 279, 8946-8956.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8946-8956
    • Fraser, C.S.1    Lee, J.Y.2    Mayeur, G.L.3    Bushell, M.4    Doudna, J.A.5    Hershey, J.W.6
  • 9
    • 77956713468 scopus 로고    scopus 로고
    • The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons
    • Chiu, W.L.; Wagner, S.; Herrmannova, A.; Burela, L.; Zhang, F.; Saini, A.K.; Valasek, L.; Hinnebusch, A.G. The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol. Cell. Biol. 2010, 30, 4415-4434.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4415-4434
    • Chiu, W.L.1    Wagner, S.2    Herrmannova, A.3    Burela, L.4    Zhang, F.5    Saini, A.K.6    Valasek, L.7    Hinnebusch, A.G.8
  • 11
    • 79953675393 scopus 로고    scopus 로고
    • eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism
    • Hilbert, M.; Kebbel, F.; Gubaev, A.; Klostermeier, D. eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucleic Acids Res. 2011, 39, 2260-2270.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2260-2270
    • Hilbert, M.1    Kebbel, F.2    Gubaev, A.3    Klostermeier, D.4
  • 13
    • 80052965200 scopus 로고    scopus 로고
    • Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B
    • Ozes, A.R.; Feoktistova, K.; Avanzino, B.C.; Fraser, C.S. Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. J. Mol. Biol. 2011, 412, 674-687.
    • (2011) J. Mol. Biol. , vol.412 , pp. 674-687
    • Ozes, A.R.1    Feoktistova, K.2    Avanzino, B.C.3    Fraser, C.S.4
  • 14
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever, T.E. Gene-specific regulation by general translation factors. Cell 2002, 108, 545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 15
    • 33750042335 scopus 로고    scopus 로고
    • 12 The eIF2α kinases
    • In 3rd ed.; Mathews, M., Sonenberg, N., Hershey, J.W.B., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Dever, T.E.; Dar, A.C.; Sicheri, F. 12 The eIF2α kinases. In Translational Control in Biology and Medicine, 3rd ed.; Mathews, M., Sonenberg, N., Hershey, J.W.B., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 2007.
    • (2007) Translational Control in Biology and Medicine
    • Dever, T.E.1    Dar, A.C.2    Sicheri, F.3
  • 17
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud, C.G. eIF2 and the control of cell physiology. Semin. Cell Dev. Biol. 2005, 16, 3-12.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 18
    • 34247111608 scopus 로고    scopus 로고
    • 13 eIF2α phosphorylation in cellular stress responses and disease
    • In Mathews, M., Sonenberg, N., Hershey, J.W.B., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Ron, D.; Harding, H.P. 13 eIF2α phosphorylation in cellular stress responses and disease. In Translational Control in Biology and Medicine; Mathews, M., Sonenberg, N., Hershey, J.W.B., Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 2007.
    • (2007) Translational Control in Biology and Medicine
    • Ron, D.1    Harding, H.P.2
  • 19
    • 80053894083 scopus 로고    scopus 로고
    • Phosphorylation of human eukaryotic initiation factor 2γ: Novel site identification and targeted PKC involvement
    • Andaya, A.; Jia, W.; Sokabe, M.; Fraser, C.S.; Hershey, J.W.; Leary, J.A. Phosphorylation of human eukaryotic initiation factor 2γ: Novel site identification and targeted PKC involvement. J. Proteome Res. 2011, 10, 4613-4623.
    • (2011) J. Proteome Res. , vol.10 , pp. 4613-4623
    • Andaya, A.1    Jia, W.2    Sokabe, M.3    Fraser, C.S.4    Hershey, J.W.5    Leary, J.A.6
  • 20
    • 0034091753 scopus 로고    scopus 로고
    • Quantitative in vitro kinase reaction as a guide for phosphoprotein analysis by mass spectrometry
    • Goodlett, D.R.; Aebersold, R.; Watts, J.D. Quantitative in vitro kinase reaction as a guide for phosphoprotein analysis by mass spectrometry. Rapid Commun. Mass Spectrom. 2000, 14, 344-348.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 344-348
    • Goodlett, D.R.1    Aebersold, R.2    Watts, J.D.3
  • 21
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S.P.; Rist, B.; Gerber, S.A.; Turecek, F.; Gelb, M.H.; Aebersold, R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17, 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 22
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 2006, 7, 952-958.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 952-958
    • Mann, M.1
  • 23
    • 15344341157 scopus 로고    scopus 로고
    • Stable isotope-free relative and absolute quantitation of protein phosphorylation stoichiometry by MS
    • Steen, H.; Jebanathirajah, J.A.; Springer, M.; Kirschner, M.W. Stable isotope-free relative and absolute quantitation of protein phosphorylation stoichiometry by MS. Proc. Natl. Acad. Sci. USA 2005, 102, 3948-3953.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3948-3953
    • Steen, H.1    Jebanathirajah, J.A.2    Springer, M.3    Kirschner, M.W.4
  • 27
    • 84857886553 scopus 로고    scopus 로고
    • Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags
    • Jia, W.; Andaya, A.; Leary, J.A. Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags. Anal. Chem. 2012, 84, 2466-2473.
    • (2012) Anal. Chem. , vol.84 , pp. 2466-2473
    • Jia, W.1    Andaya, A.2    Leary, J.A.3
  • 28
    • 44649189063 scopus 로고    scopus 로고
    • An efficient method for dephosphorylation of phosphopeptides by cerium oxide
    • Tan, F.; Zhang, Y.; Wang, J.; Wei, J.; Cai, Y.; Qian, X. An efficient method for dephosphorylation of phosphopeptides by cerium oxide. J. Mass Spectrom. 2008, 43, 628-632.
    • (2008) J. Mass Spectrom. , vol.43 , pp. 628-632
    • Tan, F.1    Zhang, Y.2    Wang, J.3    Wei, J.4    Cai, Y.5    Qian, X.6
  • 30
    • 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.; Hershey, J.W. An oncogenic role for the phosphorylated h-subunit of human translation initiation factor eIF3. J. Biol. Chem. 2008, 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.5
  • 32
    • 1642304746 scopus 로고    scopus 로고
    • X-ray structure of translation initiation factor eIF2γ: Implications for tRNA and eIF2alpha binding
    • Roll-Mecak, A.; Alone, P.; Cao, C.; Dever, T.E.; Burley, S.K. X-ray structure of translation initiation factor eIF2γ: Implications for tRNA and eIF2alpha binding. J. Biol. Chem. 2004, 279, 10634-10642.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10634-10642
    • Roll-Mecak, A.1    Alone, P.2    Cao, C.3    Dever, T.E.4    Burley, S.K.5
  • 33
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the gamma subunit in an archaeal aIF2 α γ heterodimer
    • Yatime, L.; Mechulam, Y.; Blanquet, S.; Schmitt, E. Structural switch of the gamma subunit in an archaeal aIF2 α γ heterodimer. Structure 2006, 14, 119-128.
    • (2006) Structure , vol.14 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 34
    • 55849085351 scopus 로고    scopus 로고
    • Translation initiation factor 2γ mutant alters start codon selection independent of Met-tRNA binding
    • Alone, P.V.; Cao, C.; Dever, T.E. Translation initiation factor 2γ mutant alters start codon selection independent of Met-tRNA binding. Mol. Cell. Biol. 2008, 28, 6877-6888.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6877-6888
    • Alone, P.V.1    Cao, C.2    Dever, T.E.3
  • 35
    • 33748350921 scopus 로고    scopus 로고
    • Structure of archaeal translational initiation factor 2βγ-GDP reveals significant conformational change of the β-subunit and switch 1 region
    • Sokabe, M.; Yao, M.; Sakai, N.; Toya, S.; Tanaka, I. Structure of archaeal translational initiation factor 2βγ-GDP reveals significant conformational change of the β-subunit and switch 1 region. Proc. Natl. Acad. Sci. USA 2006, 103, 13016-13021.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13016-13021
    • Sokabe, M.1    Yao, M.2    Sakai, N.3    Toya, S.4    Tanaka, I.5
  • 36
    • 0037007203 scopus 로고    scopus 로고
    • The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
    • Schmitt, E.; Blanquet, S.; Mechulam, Y. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 2002, 21, 1821-1832.
    • (2002) EMBO J. , vol.21 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 37
    • 71849102917 scopus 로고    scopus 로고
    • Eukaryotic and archaeal translation initiation factor 2: A heterotrimeric tRNA carrier
    • Schmitt, E.; Naveau, M.; Mechulam, Y. Eukaryotic and archaeal translation initiation factor 2: A heterotrimeric tRNA carrier. FEBS Lett. 2010, 584, 405-412.
    • (2010) FEBS Lett. , vol.584 , pp. 405-412
    • Schmitt, E.1    Naveau, M.2    Mechulam, Y.3
  • 38
    • 0035846821 scopus 로고    scopus 로고
    • Biochemical analysis of the eIF2beta gamma complex reveals a structural function for eIF2alpha in catalyzed nucleotide exchange
    • Nika, J.; Rippel, S.; Hannig, E.M. Biochemical analysis of the eIF2beta gamma complex reveals a structural function for eIF2alpha in catalyzed nucleotide exchange. J. Biol. Chem. 2001, 276, 1051-1056.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1051-1056
    • Nika, J.1    Rippel, S.2    Hannig, E.M.3
  • 39
    • 0019332795 scopus 로고
    • The α and γ subunits of initiation factor eIF-2 can be cross-linked to 18S ribosomal RNA within the quaternary initiation complex, eIF-2-Met-tRNAf GDPCP small ribosomal subunit
    • Westermann, P.; Nygard, O.; Bielka, H. The α and γ subunits of initiation factor eIF-2 can be cross-linked to 18S ribosomal RNA within the quaternary initiation complex, eIF-2-Met-tRNAf GDPCP small ribosomal subunit. Nucleic Acids Res. 1980, 8, 3065-3071.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 3065-3071
    • Westermann, P.1    Nygard, O.2    Bielka, H.3
  • 40
    • 79960979428 scopus 로고    scopus 로고
    • A large-scale method to measure absolute protein phosphorylation stoichiometries
    • Wu, R.; Haas, W.; Dephoure, N.; Huttlin, E.L.; Zhai, B.; Sowa, M.E.; Gygi, S.P. A large-scale method to measure absolute protein phosphorylation stoichiometries. Nat. Methods 2011, 8, 677-683.
    • (2011) Nat. Methods , vol.8 , pp. 677-683
    • Wu, R.1    Haas, W.2    Dephoure, N.3    Huttlin, E.L.4    Zhai, B.5    Sowa, M.E.6    Gygi, S.P.7
  • 41
    • 32944467424 scopus 로고    scopus 로고
    • The N-terminal domain of the human eIF2β subunit and the CK2 phosphorylation sites are required for its function
    • Llorens, F.; Duarri, A.; Sarro, E.; Roher, N.; Plana, M.; Itarte, E. The N-terminal domain of the human eIF2β subunit and the CK2 phosphorylation sites are required for its function. Biochem. J. 2010, 394, 227-237.
    • (2010) Biochem. J. , vol.394 , pp. 227-237
    • Llorens, F.1    Duarri, A.2    Sarro, E.3    Roher, N.4    Plana, M.5    Itarte, E.6
  • 42
    • 64549114921 scopus 로고    scopus 로고
    • Deletion of eIF2β suppresses testicular cancer incidence and causes recessive lethality in agouti-yellow mice
    • Heaney, J.D.; Michelson, M.V.; Youngren, K.K.; Lam, M.Y.; Nadeau, J.H. Deletion of eIF2β suppresses testicular cancer incidence and causes recessive lethality in agouti-yellow mice. Hum. Mol. Genet. 2009, 18, 1395-1404.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1395-1404
    • Heaney, J.D.1    Michelson, M.V.2    Youngren, K.K.3    Lam, M.Y.4    Nadeau, J.H.5
  • 43
    • 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.; Nogales, E. Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 2005, 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
  • 45
    • 77957222382 scopus 로고    scopus 로고
    • Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunit
    • Cai, Q.; Todorovic, A.; Andaya, A.; Gao, J.; Leary, J.A.; Cate, J.H. Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunit. J. Mol. Biol. 2010, 403, 185-196.
    • (2010) J. Mol. Biol. , vol.403 , pp. 185-196
    • Cai, Q.1    Todorovic, A.2    Andaya, A.3    Gao, J.4    Leary, J.A.5    Cate, J.H.6


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