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Volumn 274, Issue 1 43-1, 1998, Pages

Signal transduction pathways involved in the regulation of protein synthesis by insulin in L6 myoblasts

Author keywords

Eukaryotic initiation factor 4E; Eukaryotic initiation factor 4E binding protein; Eukaryotic initiation factor 4G; Translation initiation

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; INITIATION FACTOR 4E; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; RAPAMYCIN; WORTMANNIN;

EID: 0031951444     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.274.1.c221     Document Type: Article
Times cited : (128)

References (43)
  • 1
    • 0029981389 scopus 로고    scopus 로고
    • Regulation of both glycogen synthase and PHAS-I by insulin in rat skeletal muscle involves MAP kinase-independent and rapamycin-sensitive pathways
    • Azpiaza, I., A. R. Saltiel, A. A. DePaoli-Roach, and J. C. Lawrence. Regulation of both glycogen synthase and PHAS-I by insulin in rat skeletal muscle involves MAP kinase-independent and rapamycin-sensitive pathways. J. Biol. Chem. 271: 5033-5039, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5033-5039
    • Azpiaza, I.1    Saltiel, A.R.2    DePaoli-Roach, A.A.3    Lawrence, J.C.4
  • 2
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation
    • Beretta, L., A.-C. Gingras, Y. V. Svitkin, M. N. Hall, and N. Sonenberg. Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation. EMBO J. 15: 658-664, 1996.
    • (1996) EMBO J. , vol.15 , pp. 658-664
    • Beretta, L.1    Gingras, A.-C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 3
    • 0002663198 scopus 로고
    • Hormone-fuel interrelationships: Fed state, starvation, and diabetes mellitus
    • edited by C. R. Kahn and G. C. Weir. Malvern, PA: Lea and Febiger
    • Chipkin, S. R., K. L. Kelly, and N. B. Ruderman. Hormone-fuel interrelationships: fed state, starvation, and diabetes mellitus. In: Joslin's Diabetes Mellitus (13th ed.), edited by C. R. Kahn and G. C. Weir. Malvern, PA: Lea and Febiger, 1994, p. 97-115.
    • (1994) Joslin's Diabetes Mellitus (13th Ed.) , pp. 97-115
    • Chipkin, S.R.1    Kelly, K.L.2    Ruderman, N.B.3
  • 4
    • 0028178928 scopus 로고
    • PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase
    • Chung, J., T. C. Grammer, K. P. Lemon, A. Kazlauskas, and J. Blenis. PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase. Nature 370: 71-75, 1994.
    • (1994) Nature , vol.370 , pp. 71-75
    • Chung, J.1    Grammer, T.C.2    Lemon, K.P.3    Kazlauskas, A.4    Blenis, J.5
  • 5
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb, M. H., and E. J. Goldsmith. How MAP kinases are regulated. J. Biol. Chem. 270: 14843-14846, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-14846
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 6
    • 0027978816 scopus 로고
    • The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: Evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf
    • Cross, D. A., D. R. Alessi, J. R. Vandenheede, H. E. McDowell, H. S. Hundal, and P. Cohen. The inhibition of glycogen synthase kinase-3 by insulin or insulin-like growth factor 1 in the rat skeletal muscle cell line L6 is blocked by wortmannin, but not by rapamycin: evidence that wortmannin blocks activation of the mitogen-activated protein kinase pathway in L6 cells between Ras and Raf. Biochem. J. 303: 21-26, 1994.
    • (1994) Biochem. J. , vol.303 , pp. 21-26
    • Cross, D.A.1    Alessi, D.R.2    Vandenheede, J.R.3    McDowell, H.E.4    Hundal, H.S.5    Cohen, P.6
  • 7
    • 0030199543 scopus 로고    scopus 로고
    • Insulin-stimulated phosphorylation of initiation factor 4E is mediated by the MAP kinase pathway
    • Flynn, A., and C. G. Proud. Insulin-stimulated phosphorylation of initiation factor 4E is mediated by the MAP kinase pathway. FEBS Lett. 389: 162-166, 1996.
    • (1996) FEBS Lett. , vol.389 , pp. 162-166
    • Flynn, A.1    Proud, C.G.2
  • 8
    • 0029964974 scopus 로고    scopus 로고
    • The role of eIF-4 in cell proliferation
    • Flynn, A., and C. G. Proud. The role of eIF-4 in cell proliferation. Cancer Surv. 27: 293-310, 1996.
    • (1996) Cancer Surv. , vol.27 , pp. 293-310
    • Flynn, A.1    Proud, C.G.2
  • 9
    • 0029120591 scopus 로고
    • cAMP- and rapamycin-sensitive regulation of the association of eukaryotic initiation factor 4E and the translational regulator PHAS-I in aortic smooth muscle cells
    • Graves, L. M., K. E. Bornfeldt, G. M. Argast, E. G. Krebs, X. Kong, T. A. Lin, and J. C. Lawrence. cAMP- and rapamycin-sensitive regulation of the association of eukaryotic initiation factor 4E and the translational regulator PHAS-I in aortic smooth muscle cells. Proc. Natl. Acad. Sci. USA 92: 7222-7226, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7222-7226
    • Graves, L.M.1    Bornfeldt, K.E.2    Argast, G.M.3    Krebs, E.G.4    Kong, X.5    Lin, T.A.6    Lawrence, J.C.7
  • 10
    • 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. 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.
    • (1995) EMBO J. , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 11
    • 0027936088 scopus 로고
    • Phosphorylation of PHAS-I by mitogen-activated protein (MAP) kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes
    • Haystead, T. A. J., C. M. M. Haystead, C. Hu, T.-A. Lin, and J. C. Lawrence. Phosphorylation of PHAS-I by mitogen-activated protein (MAP) kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes. J. Biol. Chem. 269: 23185-23191, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23185-23191
    • Haystead, T.A.J.1    Haystead, C.M.M.2    Hu, C.3    Lin, T.-A.4    Lawrence, J.C.5
  • 12
    • 0025644509 scopus 로고
    • Effect of starvation and diabetes on the activity of the eukaryotic initiation factor eIF-2 in rat skeletal muscle
    • Jeffrey, I. W., F. J. Kelly, R. Duncan, J. W. B. Hershey, and V. M. Pain. Effect of starvation and diabetes on the activity of the eukaryotic initiation factor eIF-2 in rat skeletal muscle. Biochimie 72: 751-757, 1990.
    • (1990) Biochimie , vol.72 , pp. 751-757
    • Jeffrey, I.W.1    Kelly, F.J.2    Duncan, R.3    Hershey, J.W.B.4    Pain, V.M.5
  • 13
    • 0028069687 scopus 로고
    • In vitro synthesis of human protein synthesis initiation factor-4γ and its localization on 43 and 48 S initiation complexes
    • Joshi, B., R. Yan, and R. E. Rhoads. In vitro synthesis of human protein synthesis initiation factor-4γ and its localization on 43 and 48 S initiation complexes. J. Biol. Chem. 269: 2048-2055, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2048-2055
    • Joshi, B.1    Yan, R.2    Rhoads, R.E.3
  • 14
    • 0027404153 scopus 로고
    • Regulation of eukaryotic initiation factor 2B activity in muscle of diabetic rats
    • Endocrinol. Metab. 27
    • Karinch, A. M., S. R. Kimball, T. C. Vary, and L. S. Jefferson. Regulation of eukaryotic initiation factor 2B activity in muscle of diabetic rats. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E101-E108, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Karinch, A.M.1    Kimball, S.R.2    Vary, T.C.3    Jefferson, L.S.4
  • 15
    • 0022262839 scopus 로고
    • Control of peptide-chain initiation in rat skeletal muscle. Development of methods for preparation of native ribosomal subunits and analysis of the effect of insulin on formation of 40 S initiation complexes
    • Kelly, F. J., and L. S. Jefferson. Control of peptide-chain initiation in rat skeletal muscle. Development of methods for preparation of native ribosomal subunits and analysis of the effect of insulin on formation of 40 S initiation complexes. J. Biol. Chem. 260: 6677-6683, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6677-6683
    • Kelly, F.J.1    Jefferson, L.S.2
  • 17
    • 0023698079 scopus 로고
    • Effect of diabetes on guanine nucleotide exchange factor activity in skeletal muscle and heart
    • Kimball, S. R., and L. S. Jefferson. Effect of diabetes on guanine nucleotide exchange factor activity in skeletal muscle and heart. Biochem. Biophys. Res. Commun. 156: 706-711, 1988.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 706-711
    • Kimball, S.R.1    Jefferson, L.S.2
  • 18
    • 0025115652 scopus 로고
    • Mechanism of inhibition of protein synthesis by vasopressin in rat liver
    • Kimball, S. R., and L. S. Jefferson. Mechanism of inhibition of protein synthesis by vasopressin in rat liver. J. Biol. Chem. 265: 16794-16798, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16794-16798
    • Kimball, S.R.1    Jefferson, L.S.2
  • 19
    • 0029989622 scopus 로고    scopus 로고
    • Insulin and diabetes cause reciprocal changes in the association of eIF-4E and PHAS-I in rat skeletal muscle
    • Cell Physiol. 39
    • Kimball, S. R., L. S. Jefferson, P. Fadden, T. A. J. Haystead, and J. C. Lawrence, Jr. Insulin and diabetes cause reciprocal changes in the association of eIF-4E and PHAS-I in rat skeletal muscle. Am. J. Physiol. 270 (Cell Physiol. 39): C705-C709, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Kimball, S.R.1    Jefferson, L.S.2    Fadden, P.3    Haystead, T.A.J.4    Lawrence Jr., J.C.5
  • 20
    • 0030901124 scopus 로고    scopus 로고
    • Insulin stimulates protein synthesis in skeletal muscle by enhancing the association of eIF-4E and eIF-4G
    • Cell Physiol. 41
    • Kimball, S. R., C. V. Jurasinski, J. C. Lawrence, Jr., and L. S. Jefferson. Insulin stimulates protein synthesis in skeletal muscle by enhancing the association of eIF-4E and eIF-4G. Am. J. Physiol. 272 (Cell Physiol. 41): C754-C759, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Kimball, S.R.1    Jurasinski, C.V.2    Lawrence Jr., J.C.3    Jefferson, L.S.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF-4G) with picronaviral proteases. Implications for cap-dependent and cap-independent translational initiation
    • Lamphear, B. J., R. Kirchweger, T. Skern, and R. E. Rhoads. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF-4G) with picronaviral proteases. Implications for cap-dependent and cap-independent translational initiation. J. Biol. Chem. 270: 21975-21983, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 25
    • 0029095931 scopus 로고
    • Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, degradation, and phosphorylation by a rapamycin-sensitive and mitogen-activated protein kinase-independent pathway
    • Lin, T.-A., X. Kong, A. R. Saltiel, P. J. Blackshear, and J. C. Lawrence. Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, degradation, and phosphorylation by a rapamycin-sensitive and mitogen-activated protein kinase-independent pathway. J. Biol. Chem. 270: 18531-18538, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18531-18538
    • Lin, T.-A.1    Kong, X.2    Saltiel, A.R.3    Blackshear, P.J.4    Lawrence, J.C.5
  • 26
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4gamma and the translational repressers 4E-binding proteins
    • Mader, S., H. Lee, A. Pause, and N. Sonenberg. The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4gamma and the translational repressers 4E-binding proteins. Mol. Cell. Biol. 15: 4990-4997, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 27
    • 0025834130 scopus 로고
    • Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eucaryotic initiation factors eIF-4B and eIF-4E
    • Manzella, J. M., W. Rychlik, R. E. Rhoads, J. W. B. Hershey, and P. J. Blackshear. Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eucaryotic initiation factors eIF-4B and eIF-4E. J. Biol. Chem. 266: 2382-2389, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2382-2389
    • Manzella, J.M.1    Rychlik, W.2    Rhoads, R.E.3    Hershey, J.W.B.4    Blackshear, P.J.5
  • 28
    • 0030013326 scopus 로고    scopus 로고
    • Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase
    • Mendez, R., M. G. Myers, Jr., M. F. White, and R. E. Rhoads. Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase. Mol. Cell. Biol. 16: 2857-2864, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2857-2864
    • Mendez, R.1    Myers Jr., M.G.2    White, M.F.3    Rhoads, R.E.4
  • 29
    • 0025352294 scopus 로고
    • Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B, eIF-3, and ribosomal protein S6 by insulin and phorbol esters
    • Morley, S. J., and J. A. Traugh. Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B, eIF-3, and ribosomal protein S6 by insulin and phorbol esters. J. Biol. Chem. 265: 10611-10616, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10611-10616
    • Morley, S.J.1    Traugh, J.A.2
  • 30
    • 0027773079 scopus 로고
    • Stimulation of translation in 3T3-L1 cells in response to insulin and phorbol ester is directly correlated with increased phosphate labelling of initiation factor (eIF-) 4F and ribosomal protein S6
    • Morley, S. J., and J. A. Traugh. Stimulation of translation in 3T3-L1 cells in response to insulin and phorbol ester is directly correlated with increased phosphate labelling of initiation factor (eIF-) 4F and ribosomal protein S6. Biochimie 75: 985-989, 1993.
    • (1993) Biochimie , vol.75 , pp. 985-989
    • Morley, S.J.1    Traugh, J.A.2
  • 31
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain, V. M. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem. 236: 747-771, 1996.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 32
    • 0024544515 scopus 로고
    • Indomethacin inhibits the insulin-induced increases in RNA and protein synthesis in L6 skeletal muscle myoblasts
    • Palmer, R. M., and P. A. Bain. Indomethacin inhibits the insulin-induced increases in RNA and protein synthesis in L6 skeletal muscle myoblasts. Prostaglandins 37: 193-203, 1989.
    • (1989) Prostaglandins , vol.37 , pp. 193-203
    • Palmer, R.M.1    Bain, P.A.2
  • 33
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A., G. J. Belsham, A.-C. Gingras, O. Donze, T.-A. Lin, J. C. Lawrence, and N. Sonenberg. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature 371: 762-767, 1994.
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.-C.3    Donze, O.4    Lin, T.-A.5    Lawrence, J.C.6    Sonenberg, N.7
  • 34
    • 0028008882 scopus 로고
    • Molecular mechanisms in the control of translation by hormones and growth factors
    • Redpath, N. T., and C. G. Proud. Molecular mechanisms in the control of translation by hormones and growth factors. Biochim. Biophys. Acta 1220: 147-162, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 147-162
    • Redpath, N.T.1    Proud, C.G.2
  • 35
    • 0026757618 scopus 로고
    • Ras transformation of cloned rat embryo fibroblasts results in increased rates of protein synthesis and phosphorylation of eukaryotic initiation factor 4E
    • Rinker-Schaeffer, C. W., V. Austin, S. Zimmer, and R. E. Rhoads. Ras transformation of cloned rat embryo fibroblasts results in increased rates of protein synthesis and phosphorylation of eukaryotic initiation factor 4E. J. Biol. Chem. 267: 10659-10664, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10659-10664
    • Rinker-Schaeffer, C.W.1    Austin, V.2    Zimmer, S.3    Rhoads, R.E.4
  • 36
    • 0023035238 scopus 로고
    • Influence of anabolic agents on protein synthesis and degradation in muscle cells grown in culture
    • Roeder, R. A., S. D. Thorpe, F. M. Byers, G. T. Schelling, and J. M. Gunn. Influence of anabolic agents on protein synthesis and degradation in muscle cells grown in culture. Growth 50: 485-495, 1986.
    • (1986) Growth , vol.50 , pp. 485-495
    • Roeder, R.A.1    Thorpe, S.D.2    Byers, F.M.3    Schelling, G.T.4    Gunn, J.M.5
  • 37
    • 0025222680 scopus 로고
    • Increased rate of phosphorylation-dephosphorylation of the translational initiation factor eIF-4E correlates with the induction of protein and glycoprotein biosynthesis in activated B lymphocytes
    • Rychlik, W., J. S. Rush, R. E. Rhoads, and C. J. Waechter. Increased rate of phosphorylation-dephosphorylation of the translational initiation factor eIF-4E correlates with the induction of protein and glycoprotein biosynthesis in activated B lymphocytes. J. Biol. Chem. 265: 19467-19471, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19467-19471
    • Rychlik, W.1    Rush, J.S.2    Rhoads, R.E.3    Waechter, C.J.4
  • 38
    • 0030018849 scopus 로고    scopus 로고
    • Inhibition of growth factor-induced protein synthesis by a selective MEK inhibitor in aortic smooth muscle cells
    • Servant, M. J., E. Giasson, and S. Meloche. Inhibition of growth factor-induced protein synthesis by a selective MEK inhibitor in aortic smooth muscle cells. J. Biol. Chem. 271: 16047-16052, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16047-16052
    • Servant, M.J.1    Giasson, E.2    Meloche, S.3
  • 39
    • 0029928596 scopus 로고    scopus 로고
    • Cyclic AMP stimulates protein synthesis in L6 myoblasts and its effects are additive to those of insulin, vasopressin, and 12-O-tetradecanoylphorbol-13-acetate. Possible involvement of mitogen activated protein kinase
    • Thompson, M. G., S. C. Mackie, A. Thom, D. G. Hazlerigg, K. S. Morrison, and R. M. Palmer. Cyclic AMP stimulates protein synthesis in L6 myoblasts and its effects are additive to those of insulin, vasopressin, and 12-O-tetradecanoylphorbol-13-acetate. Possible involvement of mitogen activated protein kinase. Biochim. Biophys. Acta 1311: 37-44, 1996.
    • (1996) Biochim. Biophys. Acta , vol.1311 , pp. 37-44
    • Thompson, M.G.1    Mackie, S.C.2    Thom, A.3    Hazlerigg, D.G.4    Morrison, K.S.5    Palmer, R.M.6
  • 40
    • 0029074749 scopus 로고
    • Evidence that protein kinase C and mitogen activated protein kinase are not involved in the mechanism by which insulin stimulates translation in L6 myoblasts
    • Thompson, M. G., M. Pascal, S. C. Mackie, A. Thom, K. S. Morrison, F. R. C. Backwell, and R. M. Palmer. Evidence that protein kinase C and mitogen activated protein kinase are not involved in the mechanism by which insulin stimulates translation in L6 myoblasts. Biosci. Rep. 15: 37-46, 1995.
    • (1995) Biosci. Rep. , vol.15 , pp. 37-46
    • Thompson, M.G.1    Pascal, M.2    Mackie, S.C.3    Thom, A.4    Morrison, K.S.5    Backwell, F.R.C.6    Palmer, R.M.7
  • 41
    • 0029984354 scopus 로고    scopus 로고
    • 4E-BP1 phosphorylation is mediated by FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase
    • Von Manteuffel, S. R., A.-C. Gingras, X.-F. Ming, N. Sonenberg, and G. Thomas. 4E-BP1 phosphorylation is mediated by FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase. Proc. Natl. Acad. Sci. USA 93: 4076-4080, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4076-4080
    • Von Manteuffel, S.R.1    Gingras, A.-C.2    Ming, X.-F.3    Sonenberg, N.4    Thomas, G.5
  • 42
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh, G. I., and C. G. Proud. Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. 294: 625-629, 1993.
    • (1993) Biochem. J. , vol.294 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 43
    • 0028939115 scopus 로고
    • Multiple independent inputs are required for activation of the p70 S6 kinase
    • Weng, Q.-P., K. Andrabi, M. T. Kozlowski, J. R. Grove, and J. Avruch. Multiple independent inputs are required for activation of the p70 S6 kinase. Mol. Cell. Biol. 15: 2333-2340, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2333-2340
    • Weng, Q.-P.1    Andrabi, K.2    Kozlowski, M.T.3    Grove, J.R.4    Avruch, J.5


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