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Volumn 31, Issue 14, 2011, Pages 2947-2959

Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase Cα regulates eIF4G1 binding to Mnk1

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1; INITIATION FACTOR 4E; INITIATION FACTOR 4G; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 11; MITOGEN ACTIVATED PROTEIN KINASE SIGNAL INTEGRATING KINASE; PROTEIN KINASE C ALPHA; PROTEIN SERINE THREONINE KINASE; RAS PROTEIN; UNCLASSIFIED DRUG;

EID: 79960383717     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05589-11     Document Type: Article
Times cited : (60)

References (44)
  • 1
    • 36549040859 scopus 로고    scopus 로고
    • The selectivity of protein kinase inhibitors: a further update
    • Bain, J., et al. 2007. The selectivity of protein kinase inhibitors: a further update. Biochem. J. 408:297-315.
    • (2007) Biochem. J. , vol.408 , pp. 297-315
    • Bain, J.1
  • 2
    • 33646341222 scopus 로고    scopus 로고
    • Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1
    • Bellsolell, L., P. F. Cho-Park, F. Poulin, N. Sonenberg, and S. K. Burley. 2006. Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. Structure 14:913-923.
    • (2006) Structure , vol.14 , pp. 913-923
    • Bellsolell, L.1    Cho-Park, P.F.2    Poulin, F.3    Sonenberg, N.4    Burley, S.K.5
  • 3
    • 0030881836 scopus 로고    scopus 로고
    • Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin
    • Brunn, G. J., et al. 1997. Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin. Science 277:99-101.
    • (1997) Science , vol.277 , pp. 99-101
    • Brunn, G.J.1
  • 4
    • 0036272304 scopus 로고    scopus 로고
    • Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons
    • Byrd, M. P., M. Zamora, and R. E. Lloyd. 2002. Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons. Mol. Cell. Biol. 22:4499-4511.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4499-4511
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 5
    • 33646159052 scopus 로고    scopus 로고
    • Immunohistochemical mapping of total and phosphorylated eukaryotic initiation factor 4G in rat hippocampus following global brain ischemia and reperfusion
    • DeGracia, D. J., J. A. Rafols, S. J. Morley, and F. Kayali. 2006. Immunohistochemical mapping of total and phosphorylated eukaryotic initiation factor 4G in rat hippocampus following global brain ischemia and reperfusion. Neuroscience 139:1235-1248.
    • (2006) Neuroscience , vol.139 , pp. 1235-1248
    • DeGracia, D.J.1    Rafols, J.A.2    Morley, S.J.3    Kayali, F.4
  • 6
    • 49449085504 scopus 로고    scopus 로고
    • A quantitative atlas of mitotic phosphorylation
    • Dephoure, N., et al. 2008. A quantitative atlas of mitotic phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 105:10762-10767.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10762-10767
    • Dephoure, N.1
  • 7
    • 70449727860 scopus 로고    scopus 로고
    • Domain-dependent interaction of eukaryotic initiation factor eIF4A for binding to middle and C-terminal domains of eIF4G
    • Fujita, Y., et al. 2009. Domain-dependent interaction of eukaryotic initiation factor eIF4A for binding to middle and C-terminal domains of eIF4G. J. Biochem. 146:359-368.
    • (2009) J. Biochem. , vol.146 , pp. 359-368
    • Fujita, Y.1
  • 8
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
    • Fukunaga, R., and T. Hunter. 1997. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 16:1921-1933.
    • (1997) EMBO J , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 9
    • 77956275419 scopus 로고    scopus 로고
    • eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression
    • Furic, L., et al. 2010. eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression. Proc. Natl. Acad. Sci. U. S. A. 107:14134-14139.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14134-14139
    • Furic, L.1
  • 10
    • 66349106471 scopus 로고    scopus 로고
    • Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach
    • Gauci, S., et al. 2009. Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. 81:4493-4501.
    • (2009) Anal. Chem. , vol.81 , pp. 4493-4501
    • Gauci, S.1
  • 11
    • 0030949418 scopus 로고    scopus 로고
    • Activation of protein kinase C subtypes alpha, gamma, delta, epsilon, zeta, and eta by tumor-promoting and nontumorpromoting agents
    • Geiges, D., et al. 1997. Activation of protein kinase C subtypes alpha, gamma, delta, epsilon, zeta, and eta by tumor-promoting and nontumorpromoting agents. Biochem. Pharmacol. 53:865-875.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 865-875
    • Geiges, D.1
  • 12
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras, A. C., B. Raught, and N. Sonenberg. 1999. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68:913-963.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 13
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat, A., S. Mader, A. Pause, and N. Sonenberg. 1995. Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J. 14:5701-5709.
    • (1995) EMBO J , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 14
    • 33646124490 scopus 로고    scopus 로고
    • mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin
    • Harris, T. E., et al. 2006. mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin. EMBO J. 25:1659-1668.
    • (2006) EMBO J , vol.25 , pp. 1659-1668
    • Harris, T.E.1
  • 15
    • 0034646657 scopus 로고    scopus 로고
    • Distinct signalling pathways mediate insulin and phorbol ester-stimulated eukaryotic initiation factor 4F assembly and protein synthesis in HEK 293 cells
    • Herbert, T. P., G. R. Kilhams, I. H. Batty, and C. G. Proud. 2000. Distinct signalling pathways mediate insulin and phorbol ester-stimulated eukaryotic initiation factor 4F assembly and protein synthesis in HEK 293 cells. J. Biol. Chem. 275:11249-11256.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11249-11256
    • Herbert, T.P.1    Kilhams, G.R.2    Batty, I.H.3    Proud, C.G.4
  • 16
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • N. Sonenberg, J. W. Hershey, and M. B. Mathews (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hershey, J. W., and W. C. Merrick. 2000. Pathway and mechanism of initiation of protein synthesis, p. 637-654. In N. Sonenberg, J. W. Hershey, and M. B. Mathews (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational control of gene expression , pp. 637-654
    • Hershey, J.W.1    Merrick, W.C.2
  • 18
    • 52949088660 scopus 로고    scopus 로고
    • Activation of cap-independent translation by variant eukaryotic initiation factor 4G in vivo
    • Kaiser, C., et al. 2008. Activation of cap-independent translation by variant eukaryotic initiation factor 4G in vivo. RNA. 14:2170-2182.
    • (2008) RNA , vol.14 , pp. 2170-2182
    • Kaiser, C.1
  • 19
    • 34250902930 scopus 로고    scopus 로고
    • Targeting the protein kinase C family: are we there yet?
    • Mackay, H. J., and C. J. Twelves. 2007. Targeting the protein kinase C family: are we there yet? Nat. Rev. Cancer. 7:554-562.
    • (2007) Nat. Rev. Cancer. , vol.7 , pp. 554-562
    • Mackay, H.J.1    Twelves, C.J.2
  • 20
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano, J., A. C. Gingras, N. Sonenberg, and S. K. Burley. 1999. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell 3:707-716.
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 21
    • 0035105502 scopus 로고    scopus 로고
    • A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery
    • Marcotrigiano, J., et al. 2001. A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery. Mol. Cell 7:193-203.
    • (2001) Mol. Cell , vol.7 , pp. 193-203
    • Marcotrigiano, J.1
  • 22
    • 59049092956 scopus 로고    scopus 로고
    • Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation
    • Marintchev, A., et al. 2009. Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation. Cell 136:447-460.
    • (2009) Cell , vol.136 , pp. 447-460
    • Marintchev, A.1
  • 23
    • 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 G. Wagner. 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
  • 24
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region
    • Morino, S., H. Imataka, Y. V. Svitkin, T. V. Pestova, and N. Sonenberg. 2000. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region. Mol. Cell. Biol. 20:468-477.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 468-477
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 25
    • 0031012892 scopus 로고    scopus 로고
    • Determination of the specific substrate sequence motifs of protein kinase C isozymes
    • Nishikawa, K., A. Toker, F. J. Johannes, Z. Songyang, and L. C. Cantley. 1997. Determination of the specific substrate sequence motifs of protein kinase C isozymes. J. Biol. Chem. 272:952-960.
    • (1997) J. Biol. Chem. , vol.272 , pp. 952-960
    • Nishikawa, K.1    Toker, A.2    Johannes, F.J.3    Songyang, Z.4    Cantley, L.C.5
  • 26
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., et al. 2006. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1
  • 27
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., et al. 1994. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371:762-767.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1
  • 28
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E
    • Pyronnet, S., et al. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J. 18:270-279.
    • (1999) EMBO J , vol.18 , pp. 270-279
    • Pyronnet, S.1
  • 29
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • Raught, B., et al. 2000. Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19: 434-444.
    • (2000) EMBO J , vol.19 , pp. 434-444
    • Raught, B.1
  • 30
    • 4544384577 scopus 로고    scopus 로고
    • Tumorpromoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux, P. P., B. A. Ballif, R. Anjum, S. P. Gygi, and J. Blenis. 2004. Tumorpromoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc. Natl. Acad. Sci. U. S. A. 101:13489-13494.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 31
    • 34347242470 scopus 로고    scopus 로고
    • RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation
    • Roux, P. P., et al. 2007. RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation. J. Biol. Chem. 282:14056-14064.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14056-14064
    • Roux, P.P.1
  • 32
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J., et al. 2005. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 23:94-101.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1
  • 33
    • 33745570504 scopus 로고    scopus 로고
    • The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity
    • Shahbazian, D., et al. 2006. The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity. EMBO J. 25:2781-2791.
    • (2006) EMBO J , vol.25 , pp. 2781-2791
    • Shahbazian, D.1
  • 34
    • 34548278926 scopus 로고    scopus 로고
    • Roles of mitogen-activated protein kinase signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E phosphorylation
    • Shenberger, J. S., et al. 2007. Roles of mitogen-activated protein kinase signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E phosphorylation. Int. J. Biochem. Cell Biol. 39:1828-1842.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1828-1842
    • Shenberger, J.S.1
  • 35
    • 77957852191 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by mitogen-activated protein kinase occurs through modulation of Mnk1-eIF4G interaction
    • Shveygert, M., C. Kaiser, S. S. Bradrick, and M. Gromeier. 2010. Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by mitogen-activated protein kinase occurs through modulation of Mnk1-eIF4G interaction. Mol. Cell. Biol. 30:5160-5167.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5160-5167
    • Shveygert, M.1    Kaiser, C.2    Bradrick, S.S.3    Gromeier, M.4
  • 36
    • 0036288496 scopus 로고    scopus 로고
    • The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions
    • Slater, S. J., C. Ho, and C. D. Stubbs. 2002. The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions. Chem. Phys. Lipids 116:75-91.
    • (2002) Chem. Phys. Lipids , vol.116 , pp. 75-91
    • Slater, S.J.1    Ho, C.2    Stubbs, C.D.3
  • 37
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1
    • Songyang, Z., et al. 1996. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Mol. Cell. Biol. 16:6486-6493.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1
  • 38
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg, S. F. 2008. Structural basis of protein kinase C isoform function. Physiol. Rev. 88:1341-1378.
    • (2008) Physiol. Rev. , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 39
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax, J. A., and J. E. Ferrell, Jr. 2007. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 8:530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr., J.E.2
  • 40
    • 77956271160 scopus 로고    scopus 로고
    • Combined deficiency for MAP kinase-interacting kinase 1 and 2 (Mnk1 and Mnk2) delays tumor development
    • Ueda, T., et al. 2010. Combined deficiency for MAP kinase-interacting kinase 1 and 2 (Mnk1 and Mnk2) delays tumor development. Proc. Natl. Acad. Sci. U. S. A. 107:13984-13990.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 13984-13990
    • Ueda, T.1
  • 41
    • 0030977269 scopus 로고    scopus 로고
    • Mitogenactivated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz, A. J., A. Flynn, C. G. Proud, and J. A. Cooper. 1997. Mitogenactivated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 16:1909-1920.
    • (1997) EMBO J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3    Cooper, J.A.4
  • 42
    • 0034194092 scopus 로고    scopus 로고
    • Identification of PKC-isoformspecific biological actions using pharmacological approaches
    • Way, K. J., E. Chou, and G. L. King. 2000. Identification of PKC-isoformspecific biological actions using pharmacological approaches. Trends Pharmacol. Sci. 21:181-187.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 181-187
    • Way, K.J.1    Chou, E.2    King, G.L.3
  • 43
    • 37249042829 scopus 로고    scopus 로고
    • Dissecting eIF4E action in tumorigenesis
    • Wendel, H. G., et al. 2007. Dissecting eIF4E action in tumorigenesis. Genes Dev. 21:3232-3237.
    • (2007) Genes Dev , vol.21 , pp. 3232-3237
    • Wendel, H.G.1
  • 44
    • 0037131411 scopus 로고    scopus 로고
    • Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs
    • Zhang, H., et al. 2002. Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs. J. Biol. Chem. 277:39379-39387.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39379-39387
    • Zhang, H.1


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