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Volumn 5, Issue 211, 2012, Pages

MNK2 inhibits eIF4G activation through a pathway involving serine-arginine-rich protein kinase in skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; INITIATION FACTOR 4G; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE 1; RAPAMYCIN; S6 KINASE; SERINE; SERINE ARGININE RICH PROTEIN; SMALL INTERFERING RNA; SOMATOMEDIN C; DEXAMETHASONE; MKNK1 PROTEIN, MOUSE; MKNK2 PROTEIN, MOUSE; PROTEIN SERINE THREONINE KINASE; SRPK1 PROTEIN, MOUSE; TARGET OF RAPAMYCIN KINASE;

EID: 84857183328     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002466     Document Type: Article
Times cited : (32)

References (49)
  • 3
    • 63249134179 scopus 로고    scopus 로고
    • MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines
    • A. Csibi, M. P. Leibovitch, K. Cornille, L.A. Tintignac, S.A. Leibovitch, MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines. J. Biol. Chem. 284, 4413-4421 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4413-4421
    • Csibi, A.1    Leibovitch, M.P.2    Cornille, K.3    Tintignac, L.A.4    Leibovitch, S.A.5
  • 6
    • 70350418625 scopus 로고    scopus 로고
    • MTOR signaling at a glance
    • M. Laplante, D. M. Sabatini, mTOR signaling at a glance. J. Cell Sci. 122, 3589-3594 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 7
    • 0034635444 scopus 로고    scopus 로고
    • Activation of p70 ribosomal protein S6 kinase is an essential step in the DNA damage-dependent signaling pathway responsible for the ultraviolet B-mediated increase in interstitial collagenase (MMP-1) and stromelysin-1 (MMP-3) protein levels in human dermal fibroblasts
    • P. Brenneisen, J. Wenk, M. Wlaschek, T. Krieg, K. Scharffetter-Kochanek, Activation of p70 ribosomal protein S6 kinase is an essential step in the DNA damage-dependent signaling pathway responsible for the ultraviolet B-mediated increase in interstitial collagenase (MMP-1) and stromelysin-1 (MMP-3) protein levels in human dermal fibroblasts. J. Biol. Chem. 275, 4336-4344 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4336-4344
    • Brenneisen, P.1    Wenk, J.2    Wlaschek, M.3    Krieg, T.4    Scharffetter-Kochanek, K.5
  • 10
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • K. Hara, K. Yonezawa, Q. P. Weng, M. T. Kozlowski, C. Belham, J. Avruch, Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J. Biol. Chem. 273, 14484-14494 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 11
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • B. T. Navé, M. Ouwens, D. J. Withers, D. R. Alessi, P. R. Shepherd, Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 344 (Pt. 2), 427-431 (1999).
    • (1999) Biochem. J. , vol.344 , Issue.PART 2 , pp. 427-431
    • Navé, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 12
    • 0030806524 scopus 로고    scopus 로고
    • The insulin-induced signalling pathway leading to S6 and initiation factor 4E binding protein 1 phosphorylation bifurcates at a rapamycin-sensitive point immediately upstream of p70s6k
    • S. R. von Manteuffel, P. B. Dennis, N. Pullen, A. C. Gingras, N. Sonenberg, G. Thomas, The insulin-induced signalling pathway leading to S6 and initiation factor 4E binding protein 1 phosphorylation bifurcates at a rapamycin-sensitive point immediately upstream of p70s6k. Mol. Cell. Biol. 17, 5426-5436 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5426-5436
    • Von Manteuffel, S.R.1    Dennis, P.B.2    Pullen, N.3    Gingras, A.C.4    Sonenberg, N.5    Thomas, G.6
  • 13
    • 77951487050 scopus 로고    scopus 로고
    • Signaling pathways perturbing muscle mass
    • D. J. Glass, Signaling pathways perturbing muscle mass. Curr. Opin. Clin. Nutr. Metab. Care 13, 225-229 (2010).
    • (2010) Curr. Opin. Clin. Nutr. Metab. Care , vol.13 , pp. 225-229
    • Glass, D.J.1
  • 14
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • R. J. Jackson, C. U. Hellen, T. V. Pestova, The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11, 113-127 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 15
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E
    • S. Pyronnet, H. Imataka, A. C. Gingras, R. Fukunaga, T. Hunter, N. Sonenberg, Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. EMBO J. 18, 270-279 (1999).
    • (1999) EMBO J. , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 16
    • 0035133659 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells
    • G. C. Scheper, N. A. Morrice, M. Kleijn, C. G. Proud, The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells. Mol. Cell. Biol. 21, 743-754 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 743-754
    • Scheper, G.C.1    Morrice, N.A.2    Kleijn, M.3    Proud, C.G.4
  • 17
    • 0037781584 scopus 로고    scopus 로고
    • Conducting the initiation of protein synthesis: The role of eIF4G
    • D. Prévôt, J. L. Darlix, T. Ohlmann, Conducting the initiation of protein synthesis: The role of eIF4G. Biol. Cell 95, 141-156 (2003).
    • (2003) Biol. Cell , vol.95 , pp. 141-156
    • Prévôt, D.1    Darlix, J.L.2    Ohlmann, T.3
  • 18
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • A. C. Gingras, B. Raught, N. Sonenberg, Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15, 807-826 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 19
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • J. D. Richter, N. Sonenberg, Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 433, 477-480 (2005).
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 21
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • V. Mayya, D. H. Lundgren, S. I. Hwang, K. Rezaul, L. Wu, J. K. Eng, V. Rodionov, D. K. Han, Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. 2, ra46 (2009).
    • (2009) Sci. Signal. , vol.2
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 22
    • 67650732496 scopus 로고    scopus 로고
    • Quantitative analysis of phosphopeptides in search of the disease biomarker from the hepatocellular carcinoma specimen
    • H. J. Lee, K. Na, M. S. Kwon, H. Kim, K. S. Kim, Y. K. Paik, Quantitative analysis of phosphopeptides in search of the disease biomarker from the hepatocellular carcinoma specimen. Proteomics 9, 3395-3408 (2009).
    • (2009) Proteomics , vol.9 , pp. 3395-3408
    • Lee, H.J.1    Na, K.2    Kwon, M.S.3    Kim, H.4    Kim, K.S.5    Paik, Y.K.6
  • 25
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • B. Raught, A. C. Gingras, S. P. Gygi, H. Imataka, S. Morino, A. Gradi, R. Aebersold, N. Sonenberg, Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19, 434-444 (2000).
    • (2000) EMBO J. , vol.19 , pp. 434-444
    • Raught, B.1    Gingras, A.C.2    Gygi, S.P.3    Imataka, H.4    Morino, S.5    Gradi, A.6    Aebersold, R.7    Sonenberg, N.8
  • 26
    • 34548074950 scopus 로고    scopus 로고
    • Nutrient signaling components controlling protein synthesis in striated muscle
    • T. C. Vary, C. J. Lynch, Nutrient signaling components controlling protein synthesis in striated muscle. J. Nutr. 137, 1835-1843 (2007).
    • (2007) J. Nutr. , vol.137 , pp. 1835-1843
    • Vary, T.C.1    Lynch, C.J.2
  • 27
    • 20944444016 scopus 로고    scopus 로고
    • IGF-I activates the eIF4F system in cardiac muscle in vivo
    • T. C. Vary, C. H. Lang, IGF-I activates the eIF4F system in cardiac muscle in vivo. Mol. Cell. Biochem. 272, 209-220 (2005).
    • (2005) Mol. Cell. Biochem. , vol.272 , pp. 209-220
    • Vary, T.C.1    Lang, C.H.2
  • 28
    • 18844390423 scopus 로고    scopus 로고
    • Insulin and IGF-I stimulate the formation of the eukaryotic initiation factor 4F complex and protein synthesis in C2C12 myotubes independent of availability of external amino acids
    • W. H. Shen, D. W. Boyle, P. Wisniowski, A. Bade, E. A. Liechty, Insulin and IGF-I stimulate the formation of the eukaryotic initiation factor 4F complex and protein synthesis in C2C12 myotubes independent of availability of external amino acids. J. Endocrinol. 185, 275-289 (2005).
    • (2005) J. Endocrinol. , vol.185 , pp. 275-289
    • Shen, W.H.1    Boyle, D.W.2    Wisniowski, P.3    Bade, A.4    Liechty, E.A.5
  • 29
    • 33748302991 scopus 로고    scopus 로고
    • Meal feeding stimulates phosphorylation of multiple effector proteins regulating protein synthetic processes in rat hearts
    • T. C. Vary, C. J. Lynch, Meal feeding stimulates phosphorylation of multiple effector proteins regulating protein synthetic processes in rat hearts. J. Nutr. 136, 2284-2290 (2006).
    • (2006) J. Nutr. , vol.136 , pp. 2284-2290
    • Vary, T.C.1    Lynch, C.J.2
  • 30
    • 33646079646 scopus 로고    scopus 로고
    • Meal feeding enhances formation of eIF4F in skeletal muscle: Role of increased eIF4E availability and eIF4G phosphorylation
    • T. C. Vary, C. J. Lynch, Meal feeding enhances formation of eIF4F in skeletal muscle: Role of increased eIF4E availability and eIF4G phosphorylation. Am. J. Physiol. Endocrinol. Metab. 290, E631-E642 (2006).
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.290
    • Vary, T.C.1    Lynch, C.J.2
  • 31
    • 34547632886 scopus 로고    scopus 로고
    • Regulation of muscle protein synthesis during sepsis and inflammation
    • C. H. Lang, R. A. Frost, T. C. Vary, Regulation of muscle protein synthesis during sepsis and inflammation. Am. J. Physiol. Endocrinol. Metab. 293, E453-E459 (2007).
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.293
    • Lang, C.H.1    Frost, R.A.2    Vary, T.C.3
  • 32
    • 33751220195 scopus 로고    scopus 로고
    • Cytokine-triggered decreases in levels of phosphorylated eukaryotic initiation factor 4G in skeletal muscle during sepsis
    • T. C. Vary, G. Deiter, C. H. Lang, Cytokine-triggered decreases in levels of phosphorylated eukaryotic initiation factor 4G in skeletal muscle during sepsis. Shock 26, 631-636 (2006).
    • (2006) Shock , vol.26 , pp. 631-636
    • Vary, T.C.1    Deiter, G.2    Lang, C.H.3
  • 33
    • 0043133828 scopus 로고    scopus 로고
    • The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization
    • G. C. Scheper, J. L. Parra, M. Wilson, B. Van Kollenburg, A. C. Vertegaal, Z. G. Han, C. G. Proud, The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization. Mol. Cell. Biol. 23, 5692-5705 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5692-5705
    • Scheper, G.C.1    Parra, J.L.2    Wilson, M.3    Van Kollenburg, B.4    Vertegaal, A.C.5    Han, Z.G.6    Proud, C.G.7
  • 34
    • 3242719457 scopus 로고    scopus 로고
    • Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development
    • T. Ueda, R. Watanabe-Fukunaga, H. Fukuyama, S. Nagata, R. Fukunaga, Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development. Mol. Cell. Biol. 24, 6539-6549 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6539-6549
    • Ueda, T.1    Watanabe-Fukunaga, R.2    Fukuyama, H.3    Nagata, S.4    Fukunaga, R.5
  • 36
    • 0037205409 scopus 로고    scopus 로고
    • Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site
    • M. Saitoh, N. Pullen, P. Brennan, D. Cantrell, P. B. Dennis, G. Thomas, Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site. J. Biol. Chem. 277, 20104-20112 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 20104-20112
    • Saitoh, M.1    Pullen, N.2    Brennan, P.3    Cantrell, D.4    Dennis, P.B.5    Thomas, G.6
  • 37
    • 0345732640 scopus 로고    scopus 로고
    • mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E
    • D. C. Fingar, C. J. Richardson, A. R. Tee, L. Cheatham, C. Tsou, J. Blenis, mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 24, 200-216 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 200-216
    • Fingar, D.C.1    Richardson, C.J.2    Tee, A.R.3    Cheatham, L.4    Tsou, C.5    Blenis, J.6
  • 40
    • 3042701690 scopus 로고    scopus 로고
    • Leucine regulates translation initiation in rat skeletal muscle via enhanced eIF4G phosphorylation
    • D. R. Bolster, T. C. Vary, S. R. Kimball, L. S. Jefferson, Leucine regulates translation initiation in rat skeletal muscle via enhanced eIF4G phosphorylation. J. Nutr. 134, 1704-1710 (2004).
    • (2004) J. Nutr. , vol.134 , pp. 1704-1710
    • Bolster, D.R.1    Vary, T.C.2    Kimball, S.R.3    Jefferson, L.S.4
  • 41
    • 0033808169 scopus 로고    scopus 로고
    • Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway
    • J. C. Anthony, F. Yoshizawa, T. G. Anthony, T. C. Vary, L. S. Jefferson, S. R. Kimball, Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J. Nutr. 130, 2413-2419 (2000).
    • (2000) J. Nutr. , vol.130 , pp. 2413-2419
    • Anthony, J.C.1    Yoshizawa, F.2    Anthony, T.G.3    Vary, T.C.4    Jefferson, L.S.5    Kimball, S.R.6
  • 42
    • 63749105226 scopus 로고    scopus 로고
    • mTOR and the control of whole body metabolism
    • P. Polak, M. N. Hall, mTOR and the control of whole body metabolism. Curr. Opin. Cell Biol. 21, 209-218 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 209-218
    • Polak, P.1    Hall, M.N.2
  • 43
    • 27744569843 scopus 로고    scopus 로고
    • mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • M. K. Holz, B. A. Ballif, S. P. Gygi, J. Blenis, mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123, 569-580 (2005).
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 44
    • 79751504755 scopus 로고    scopus 로고
    • Phosphorylation mechanism and structure of serine-arginine protein kinases
    • G. Ghosh, J. A. Adams, Phosphorylation mechanism and structure of serine-arginine protein kinases. FEBS J. 278, 587-597 (2011).
    • (2011) FEBS J. , vol.278 , pp. 587-597
    • Ghosh, G.1    Adams, J.A.2
  • 45
    • 79751475964 scopus 로고    scopus 로고
    • Serine-arginine protein kinases: A small protein kinase family with a large cellular presence
    • T. Giannakouros, E. Nikolakaki, I. Mylonis, E. Georgatsou, Serine-arginine protein kinases: A small protein kinase family with a large cellular presence. FEBS J. 278, 570-586 (2011).
    • (2011) FEBS J. , vol.278 , pp. 570-586
    • Giannakouros, T.1    Nikolakaki, E.2    Mylonis, I.3    Georgatsou, E.4
  • 46
    • 0035224873 scopus 로고    scopus 로고
    • Phosphorylation of mammalian eIF4E by Mnk1 and Mnk2: Tantalizing prospects for a role in translation
    • M. Mahalingam, J. A. Cooper, Phosphorylation of mammalian eIF4E by Mnk1 and Mnk2: Tantalizing prospects for a role in translation. Prog. Mol. Subcell. Biol. 27, 132-142 (2001).
    • (2001) Prog. Mol. Subcell. Biol. , vol.27 , pp. 132-142
    • Mahalingam, M.1    Cooper, J.A.2
  • 47
    • 0034928792 scopus 로고    scopus 로고
    • Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2
    • U. Knauf, C. Tschopp, H. Gram, Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol. Cell. Biol. 21, 5500-5511 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5500-5511
    • Knauf, U.1    Tschopp, C.2    Gram, H.3
  • 48
    • 28644439239 scopus 로고    scopus 로고
    • Inhibition of cap-dependent translation via phosphorylation of eIF4G by protein kinase Pak2
    • J. Ling, S. J. Morley, J. A. Traugh, Inhibition of cap-dependent translation via phosphorylation of eIF4G by protein kinase Pak2. EMBO J. 24, 4094-4105 (2005).
    • (2005) EMBO J. , vol.24 , pp. 4094-4105
    • Ling, J.1    Morley, S.J.2    Traugh, J.A.3
  • 49
    • 79960383717 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase Ca regulates eIF4G1 binding to Mnk1
    • M. Dobrikov, E. Dobrikova, M. Shveygert, M. Gromeier, Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase Ca regulates eIF4G1 binding to Mnk1. Mol. Cell. Biol. 31, 2947-2959 (2011).
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2947-2959
    • Dobrikov, M.1    Dobrikova, E.2    Shveygert, M.3    Gromeier, M.4


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