Eukaryotic Initiation Factor 2B and Its Role in Alterations in mRNA Translation That Occur Under a Number of Pathophysiological and Physiological Conditions

Progress in Nucleic Acid Research and Molecular Biology

Volumn 81, Issue , 2006, Pages 271-296

  Kubica, Neil ^a   Jefferson, Leonard S ^a   Kimball, Scot R ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; PROTEIN SUBUNIT;

ANIMAL; GENERAL ASPECTS OF DISEASE; GENETICS; HUMAN; METABOLISM; PROTEIN SYNTHESIS; REVIEW;

ANIMALS; DISEASE; EUKARYOTIC INITIATION FACTOR-2B; HUMANS; PROTEIN BIOSYNTHESIS; PROTEIN SUBUNITS;

EID: 33750629031     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6603(06)81007-X     Document Type: Review

References (162)

1. Safer B., Jagus R., Konieczny A., and Crouch D. The mechanism of translational inhibition in hemin-deficient lysates. In: Grunberg-Manago M., and Safer B. (Eds). "Interactions of Translational and Transcriptional Controls in the Regulation of Gene Expression" (1982), Elsevier Science Publishing Co., Inc., NY, NY 311-325
2. Chen J.-J. Heme-regulated eIF2α kinase. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds). "Translational Control of Gene Expression" (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 529-546
3. Ochoa S. Regulation of protein synthesis initiation in eucaryotes. Arch. Biochem. Biophys. 223 (1983) 325-349
4. Ralston R.O., Das A., Dasgupta A., Roy R., Palmieri S., and Gupta N.K. Protein synthesis in rabbit reticulocytes: Characteristics of a ribosomal factor that reverses inhibition of protein synthesis in heme-deficient lysates. Proc. Natl. Acad. Sci. USA 75 (1978) 4858-4862
5. Amesz H., Goumans H., Haubrich-Morree T., Voorma H.O., and Benne R. Purification and characterization of a protein factor that reverses the inhibition of protein synthesis by the heme-regulated translational inhibitor in rabbit reticulocyte lysates. Eur. J. Biochem. 98 (1979) 513-520
6. Panniers R., and Henshaw E.C. A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in ehrlich ascites tumor cells and its regulation by eukaryotic initiation factor 2 phosphorylation. J. Biol. Chem. 258 (1983) 7928-7934
7. Konieczny A., and Safer B. Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange activity during protein synthesis initiation. J. Biol. Chem. 258 (1983) 3402-3408
8. Hinnebusch A.G. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. In: Sonenberg N., Hershey, J.W.B., and Mathews M.B. (Eds). "Translational Control of Gene Expression" (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 185-243
9. Farrell P.J., Balkow K., Hunt T., Jackson R.J., and Trachsel H. Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis. Cell 11 (1977) 187-200
10. Harding H.P., Zhang Y., and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397 (1999) 271-274
11. Shi Y., Vattem K.M., Sood R., An J., Liang J., Stramm L., and Wek R.C. Identification and characterization of pancreatic eukaryotic initiation factor 2 α-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18 (1998) 7499-7509
12. Berlanga J.J., Santoyo J., and de Haro C. Characterization of a mammalian homolog of GCN2 eukaryotic initiation factor 2α kinase. Eur. J. Biochem. 265 (1999) 754-762
13. Hinnebusch A.G., and Natarajan K. Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress. Eukaryot. Cell 1 (2002) 22-32
14. Proud C.G. eIF2 and the control of cell physiology. Semin. Cell Develop. Biol. 16 (2005) 3
15. Hinnebusch A.G. Translational control of GCN4: An in vivo barometer of initiation factor activity. Trends Biochem. Sci. 19 (1994) 409-414
16. Vattem K.M., and Wek R.C. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl. Acad. Sci. USA 101 (2004) 11269-11274
17. Vilela C., and McCarthy J.E.G. Regulation of fungal gene expression via short open reading frames in the mRNA 5′untranslated region. Mol. Microbiol. 49 (2003) 859-867
18. Zhang Z., and Dietrich F.S. Identification and characterization of upstream open reading frames (uORF) in the 5′-untranslated regions (UTR) of genes in Saccharomyces cerevisiae. Curr. Genet. 48 (2005) 77-87
19. Peri S., and Pandey A. A reassessment of the translation initiation codon in vertebrates. Trends Genet. 17 (2001) 685-687
20. Cox S., Redpath N.T., and Proud C.G. Regulation of polypeptide-chain initiation in rat skeletal muscle starvation does not alter the activity or phosphorylation state of initiation factor eIF-2. FEBS Lett. 239 (1988) 333-338
21. Jeffrey I.W., Kelly F.J., Duncan R., Hershey J.W.B., and Pain V.M. Effect of starvation and diabetes on the activity of the eukaryotic initiation factor eIF-2 in rat skeletal muscle. Biochimie 72 (1990) 751-757
22. Karinch A.M., Kimball S.R., Vary T.C., and Jefferson L.S. Regulation of eukaryotic initiation factor 2B activity in muscle of diabetic rats. Am. J. Physiol. 264 (1993) E101-E108
23. Kimball S.R., and Jefferson L.S. Effect of diabetes on guanine nucleotide exchange factor activity in skeletal muscle and heart. Biochem. Biophys. Res. Commun. 156 (1988) 706-711
24. Welsh G.I., and Proud C.G. Regulation of protein synthesis in Swiss 3T3 fibroblasts. Rapid activation of the guanine nucleotide exchange factor by insulin and growth factors. Biochem. J. 284 (1992) 19-23
25. Wang X., Janmaat M., Beugnet A., Paulin F.E., and Proud C.G. Evidence that the dephosphorylation of Ser(535) in the epsilon-subunit of eukaryotic initiation factor (eIF) 2B is insufficient for the activation of eIF2B by insulin. Biochem. J. 367 (2002) 475-481
26. Welsh G.I., Miller C.M., Loughlin A.J., Price N.T., and Proud C.G. Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett. 421 (1998) 125-130
27. Woods Y.L., Cohen P., Becker W., Jakes R., Goedert M., Wang X., and Proud C.G. The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem. J. 355 (2001) 609-615
28. Dholakia J.N., Mueser T.C., Woodley C.L., Parkhurst L.J., and Wahba A.J. The association of NADPH with the guanine nucleotide exchange factor from rabbit reticulocytes: A role of pyridine dinucleotides in eukaryotic polypeptide chain initiation. Proc. Natl. Acad. Sci. USA 83 (1986) 6746-6750
29. Kimball S.R., Mellor H., Flowers K.M., and Jefferson L.S. Role of translation initiation factor eIF-2B in the regulation of protein synthesis in mammalian cells. Prog. Nucleic Acid Res. Mol. Biol. 54 (1996) 165-196
30. Greenbaum A.L., Gumaa K.A., and McLean P. The distribution of hepatic metabolites and the control of the pathways of carbohydrate metabolism in animals of different dietary and hormonal status. Arch. Biochem. Biophys. 143 (1971) 617-663
31. Akkaraju G.R., Hansen L.J., and Jagus R. Increase in eukaryotic initiation factor 2B activity following fertilization reflects changes in redox potential. J. Biol. Chem. 266 (1991) 24451-24459
32. Abbott C.M., and Proud C.G. Translation factors: In sickness and in health. Trends Biochem. Sci. 29 (2004) 25-31
33. Pavitt G.D., Yang W., and Hinnebusch A.G. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol. 17 (1997) 1298-1313
34. Pavitt G.D., Ramaiah K.V.A., Kimball S.R., and Hinnebusch A.G. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev. 12 (1998) 514-526
35. Fabian J.R., Kimball S.R., Heinzinger N.D., and Jefferson L.S. Subunit assembly and guanine nucleotide exchange activity of eukaryotic initiation factor-2B (eIF-2B) expressed in Sf9 cells. J. Biol. Chem. 272 (1997) 12359-12365
36. Kimball S.R., Fabian J.R., Pavitt G.D., Hinnebusch A.G., and Jefferson L.S. Regulation of guanine nucleotide exchange through phosphorylation of eukaryotic initiation factor eIF2α. Role of the α- and δ-subunits of eIF2B. J. Biol. Chem. 273 (1998) 12841-12845
37. Craddock B.L., and Proud C.G. The α-subunit of the mammalian guanine nucleotide-exchange factor eIF-2B is essential for catalytic activity in vitro. Biochem. Biophys. Res. Commun. 220 (1996) 843-847
38. Williams D.D., Pavitt G.D., and Proud C.G. Characterization of the initiation factor eIF2B and its regulation in Drosophila melanogaster. J. Biol. Chem. 276 (2001) 3733-3742
39. Gomez E., Mohammad S.S., and Pavitt G.D. Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation. EMBO J. 21 (2002) 5292-5301
40. Anthony T.G., Fabian J.R., Kimball S.R., and Jefferson L.S. Identification of domains within the ε-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation. Biochim. Biophys. Acta 1492 (2000) 56-62
41. Boesen T., Mohammad S.S., Pavitt G.D., and Andersen G.R. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 279 (2004) 10584-10592
42. Fabian J.R., Kimball S.R., and Jefferson L.S. Reconstitution and purification of eukaryotic initiation factor 2B (eIF2B) expressed in Sf21 insect cells. Prot. Express. Purif. 13 (1998) 16-22
43. Kimball S.R., Heinzinger N.K., Horetsky R.L., and Jefferson L.S. Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B. J. Biol. Chem. 273 (1998) 3039-3044
44. Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., and Hinnebusch A.G. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18 (1999) 1673-1688
45. Chaikoff I.L., and Forker L.L. The antidiabetic action of insulin on nitrogen metabolism. Endocrinology 46 (1950) 319-326
46. Forker L.L., Chiakoff I.L., Entenman C., and Tarver H. Oxidation of methionine S35 to sulfate by the eviscerated dog. J. Biol. Chem. 188 (1951) 31-35
47. Forker L.L., and Chaikoff I.L. Turnover of serum proteins in diabetes as studied with S35 labeled proteins. J. Biol. Chem. 196 (1952) 829-840
48. Green M., and Miller L.L. Protein catabolism and protein synthesis in perfused livers of normal and alloxan-diabetic rats. J. Biol. Chem. 235 (1960) 3202-3208
49. Rampersad O.R., and Wool I.G. Protein synthesis by ribosomes from heart muscle: Effect of insulin and diabetes. Science 149 (1965) 1102-1103
50. Wool I.G., Rampersad O.R., and Moyer A.N. Effect of insulin and diabetes on protein synthesis by ribosomes from heart muscle. Significance for theories of the hormone's mechanism of action. Am. J. Med. 40 (1966) 716-723
51. Manchester K.L., and Young F.G. The effect of insulin on incorporation of amino acids into protein of normal rat diaphragm in vitro. Biochem. J. 70 (1958) 353-358
52. Wool I.G., and Krahl M.E. Incorporation of C14-amino acids into protein of isolated diaphragms: An effect of insulin independent of glucose entry. Am. J. Physiol. 196 (1959) 961-964
53. Wool I.G., and Krahl M.E. An effect of insulin on peptide synthesis independent of glucose or amino-acid transport. Nature 183 (1959) 1399-1400
54. Manchester K.L., and Krahl M.E. Effect of insulin on the incorporation of C14 from C14-labeled carboxylic acids and bicarbonate into the protein of isolated rat diaphragm. J. Biol. Chem. 234 (1959) 2938-2942
55. Wool I.G. Relation of effects of insulin on amino acid transport and on protein synthesis. Fed. Proc. 24 (1965) 1060-1070
56. Stirewalt W.S., and Wool I.G. Protein synthesis by heart muscle ribosomes: An effect of insulin independent of substrate transport. Science 154 (1966) 284-285
57. Wool I.G. Effect of insulin on distribution of radioactivity in protein of cell fractions from isolated rat diaphragm. Biochim. Biophys. Acta 52 (1961) 574-576
58. Eboue Bonis D., Chambaut A.M., Volfin P., and Clauser H. Action of insulin on the isolated rat diaphragm in the presence of actinomycin D and puromycin. Nature 199 (1963) 1183-1184
59. Wool I.G., and Moyer A.N. Effect of actinomycin and insulin on the metabolism of isolated rat diaphragm. Biochim. Biophys. Acta 91 (1964) 248-256
60. Fahmy L.H., and Leader D.P. The effect of diabetes and insulin on the polyadenylic acid-containing RNA of rat skeletal muscle. Biochim. Biophys. Acta 608 (1980) 344-357
61. Stirewalt W.S., Wool I.G., and Cavicchi P. The relation of RNA and protein synthesis to the sedimentation of muscle ribosomes: Effect of diabetes and insulin. Proc. Natl. Acad. Sci. USA 57 (1967) 1885-1892
62. Flaim K.E., Copenhaver M.E., and Jefferson L.S. Effects of diabetes on protein synthesis in fast- and slow-twitch rat skeletal muscle. Am. J. Physiol. 239 (1980) E88-E95
63. Karinch A.M., Kimball S.R., Vary T.C., and Jefferson L.S. Regulation of eukaryotic initiation factor-2B activity in muscle of diabetic rats. Am. J. Physiol. 264 (1993) E101-E108
64. Crozier S.J., Bolster D.R., Reiter A.K., Kimball S.R., and Jefferson L.S. β-Oxidation of free fatty acids is required to maintain translational control of protein synthesis in heart. Am. J. Physiol. 283 (2002) E1144-E1150
65. Crozier S.J., Anthony J.C., Schworer C.M., Reiter A.K., Anthony T.G., Kimball S.R., and Jefferson L.S. Tissue-specific regulation of protein synthesis by insulin and free fatty acids. Am. J. Physiol. Endocrinol. Metab. 285 (2003) E754-E762
66. Welsh G.I., and Proud C.G. Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J. 294 (1993) 625-629
67. Ramakrishna S., and Benjamin W. Insulin action rapidly decreases multifunctional protein kinase activity in rat adipose tissue. J. Biol. Chem. 263 (1988) 12677-12681
68. Sutherland C., and Cohen P. The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro. FEBS Lett. 338 (1994) 37-42
69. Sutherland C., Leighton I., and Cohen P. Inactivation of glycogen synthase kinase-3 beta by phosphorylation: New kinase connections in insulin and growth-factor signalling. Biochem. J. 296 (1993) 15-19
70. Cross D.A., Alessi D.R., Vandenheede J.R., McDowell H.E., Hundal H.S., and Cohen P. 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 (1994) 21-26
71. Welsh G.I., Foulstone E.J., Young S.W., Tavare J.M., and Proud C.G. Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase. Biochem. J. 303 (1994) 15-20
72. Burgering B.M., and Coffer P.J. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376 (1995) 599-602
73. Franke T.F., Yang S.I., Chan T.O., Datta K., Kazlauskas A., Morrison D.K., Kaplan D.R., and Tsichlis P.N. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81 (1995) 727-736
74. Cross D.A.E., Alessi D.R., Cohen P., Andjelkovich M., and Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378 (1995) 785-789
75. Cross D.A.E., Watt P.W., Shaw M., van der Kaay J., Downes C.P., Holder J.C., and Cohen P. Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue. FEBS Lett. 406 (1997) 211-215
76. Moule S.K., Edgell N.J., Welsh G.I., Diggle T.A., Proud C.G., and Denton R.M. Studies with wortmannin indicate that insulin stimulation of lipogenesis involves multiple signalling pathways. Biochem. Soc. Trans. 23 (1995) 206S
77. Hurel S.J., Rochford J.J., Borthwick A.C., Wells A.M., Vandenheede J.R., Turnbull D.M., and Yeaman S.J. Insulin action in cultured human myoblasts: Contribution of different signalling pathways to regulation of glycogen synthesis. Biochem. J. 320 (1996) 871-877
78. Welsh G.I., Stokes C.M., Wang X., Sakaue H., Ogawa W., Kasuga M., and Proud C.G. Activation of translation initiation factor eIF2B by insulin requires phosphatidyl inositol 3-kinase. FEBS Lett. 410 (1997) 418-422
79. Welsh G.I., Miller C.M., Loughlin A.J., Price N.T., and Proud C.G. Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett. 421 (1998) 125-130
80. Jefferson L.S., Fabian J.R., and Kimball S.R. Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle. Int. J. Biochem. Cell. Biol. 31 (1999) 191-200
81. Wang X., Janmaat M., Beugent A., Paulin F.E., and Proud C.G. Evidence that the dephosphorylation of Ser(535) in the epsilon-subunit of eukaryotic initiation factor (eIF) 2B is insufficient for the activation of eIF2B by insulin. Biochem. J. 367 (2002) 475-481
82. Fisher T.L., and White M.F. Signaling pathways: The benefits of good communication. Curr. Biol. 14 (2004) R1005-R1007
83. Shah O.J., Wang Z., and Hunter T. Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies. Curr. Biol. 14 (2004) 1650-1656
84. Harrington L.S., Findlay G.M., Gray A., Tolkacheva T., Wigfield S., Rebholz H., Barnett J., Leslie N.R., Cheng S., Shepherd P.R., Gout I., Downes C.P., et al. The TSC1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteins. J. Cell Biol. 166 (2004) 213-223
85. Mothe I., and Van Obberghen E. Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action. J. Biol. Chem. 271 (1996) 11222-11227
86. Rui L., Fisher T.L., Thomas J., and White M.F. Regulation of insulin/insulin-like growth factor-1 signaling by proteasome-mediated degradation of insulin receptor substrate-2. J. Biol. Chem. 276 (2001) 40362-40367
87. Um S.H., Frigerio F., Watanabe M., Picard F., Joaquin M., Sticker M., Fumagalli S., Allegrini P.R., Kozma S.C., Auwerx J., and Thomas G. Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 431 (2004) 200-205
88. Fluckey J.D., Vary T.C., Jefferson L.S., and Farrell P.A. Augmented insulin action on rates of protein synthesis after resistance exercise in rats. Am. J. Physiol. 270 (1996) E313-E319
89. Farrell P.A., Fedele M.J., Vary T.C., Kimball S.R., and Jefferson L.S. Effects of intensity of acute-resistance exercise on rates of protein synthesis in moderately diabetic rats. J. Appl. Physiol. 85 (1998) 2291-2297
90. Farrell P.A., Fedele M.J., Vary T.C., Kimball S.R., Lang C.H., and Jefferson L.S. Regulation of protein synthesis after acute resistance exercise in diabetic rats. Am. J. Physiol. 276 (1999) E721-E727
91. Fedele M.J., Hernandez J.M., Lang C.H., Vary T.C., Kimball S.R., Jefferson L.S., and Farrell P.A. Severe diabetes prohibits elevations in muscle protein synthesis after acute resistance exercise in rats. J. Appl. Physiol. 88 (2000) 102-108
92. Fedele M.J., Lang C.H., and Farrell P.A. Immunization against IGF-I prevents increases in protein synthesis in diabetic rats after resistance exercise. Am. J. Physiol. 280 (2001) E877-E885
93. Kostyak J.C., Kimball S.R., Jefferson L.S., and Farrell P.A. Severe diabetes inhibits resistance exercise-induced increase in eukaryotic initiation factor 2B activity. J. Appl. Physiol. 91 (2001) 79-84
94. Kubica N., Bolster D.R., Farrell P.A., Kimball S.R., and Jefferson L.S. Resistance exercise increases muscle protein synthesis and translation of eukaryotic initiation factor 2Bε mRNA in a mammalian target of rapamycin-dependent manner. J. Biol. Chem. 280 (2005) 7570-7580
95. Farrell P.A., Hernandez J.M., Fedele M.J., Vary T.C., Kimball S.R., and Jefferson L.S. Eukaryotic initiation factors and protein synthesis after resistance exercise in rats. J. Appl. Physiol. 88 (2000) 1036-1042
96. Markuns J.F., Wojtaszewski J.F.P., and Goodyear L.J. Insulin and exercise decrease glycogen synthase kinase-3 activity by different mechanisms in rat skeletal muscle. J. Biol. Chem. 274 (1999) 24896-24900
97. Turinsky J., and Damrau-Abney A. Akt kinases and 2-deoxyglucose uptake in rat skeletal muscles in vivo: Study with insulin and exercise. Am. J. Physiol. 276 (1999) R277-R282
98. Sakamoto K., Aschenbach W.G., Hirshman M.F., and Goodyear L.J. Akt signaling in skeletal muscle: Regulation by exercise and passive stretch. Am. J. Physiol. 285 (2003) E1081-E1088
99. Bolster D.R., Kubica N., Crozier S.J., Williamson D.L., Farrell P.A., Kimball S.R., and Jefferson L.S. Immediate response of mammalian target of rapamycin (mTOR)-mediated signalling following acute resistance exercise in rat skeletal muscle. J. Physiol. 553 (2003) 213-220
100. Atherton P.J., Babraj J., Smith K., Singh J., Rennie M.J., and Wackerhage H. Selective activation of AMPK-PGC-1α or PKB-TSC2-mTOR signaling can explain specific adaptive responses to endurance or resistance training-like electrical muscle stimulation. FASEB J. 19 (2005) 786-788
101. Kubica N., Kimball S.R., Jefferson L.S., and Farrell P.A. Alterations in the expression of mRNAs and proteins that code for species relevant to eIF2B activity after an acute bout of resistance exercise. J. Appl. Physiol. 96 (2004) 679-687
102. Hernandez J.M., Fedele M.J., and Farrell P.A. Time course evaluation of protein synthesis and glucose uptake after acute resistance exercise in rats. J. Appl. Physiol. 88 (2000) 1142-1149
103. Nader G.A., and Esser K.A. Intracellular signaling specificity in skeletal muscle in response to different modes of exercise. J. Appl. Physiol. 90 (2001) 1936-1942
104. Parkington J.D., Siebert A.P., LeBrasseur N.K., and Fielding R.A. Differential activation of mTOR signaling by contractile activity in skeletal muscle. Am. J. Physiol. 285 (2003) R1086-R1090
105. Bodine S.C., Stitt T.N., Gonzalez M., Kline W.O., Stover G.L., Bauerlein R., Zlotchenko E., Scrimgeous A., Lawrence J.C., Glass D.J., and Yancopoulos G.D. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3 (2001) 1014-1019
106. Pallafacchina G., Calabria E., Serrano A.L., Kalhovde J.M., and Schiaffino S. A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification. Proc. Natl. Acad. Sci. USA 99 (2002) 9213-9218
107. Lai K.-M.V., Gonzalez M., Poueymirou W.T., Kline W.O., Na E., Zlotchenko E., Stitt T.N., Economides A.N., Yancopoulos G.D., and Glass D.J. Conditional activation of Akt in adult skeletal muscle induces rapid hypertrophy. Mol. Cell. Biol. 24 (2004) 9295-9304
108. Gomez E., and Pavitt G.D. Identification of domains and residues within the ε subunit of eukaryotic translation initiation factor 2B (eIF2Bε) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation. Mol. Cell. Biol. 20 (2000) 3965-3976
109. Gomez E., Mohammad S.S., and Pavitt G.D. Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation. EMBO J. 21 (2002) 5292-5301
110. Boesen T., Mohammad S.S., Pavitt G.D., and Andersen G.R. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 279 (2004) 10584-10592
111. Fabian J.R., Kimball S.R., Heinzinger N.K., and Jefferson L.S. Subunit assembly and guanine nucleotide exchange activity of eukaryotic initiation factor-2B expressed in Sf9 Cells. J. Biol. Chem. 272 (1997) 12359-12365
112. Fabian J.R., Kimball S.R., and Jefferson L.S. Reconstitution and purification of eukaryotic initiation factor 2B (eIF2B) expressed in Sf21 insect cells. Prot. Express. Purif. 13 (1998) 16-22
113. Pavitt G.D., Ramaiah K.V.A., Kimball S.R., and Hinnebusch A.G. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev. 12 (1998) 514-526
114. Williams D.D., Pavitt G.D., and Proud C.G. Characterization of the initiation factor eIF2B and its regulation in Drosophila melanogaster. J. Biol. Chem. 276 (2001) 3733-3742
115. Hardt S.E., Tomita H., Katus H.A., and Sadoshima J. Phosphorylation of eukaryotic translation initiation factor 2Bε by glycogen synthase kinase-3β regulates β-adrenergic cardiac myocyte hypertrophy. Circ. Res. 94 (2004) 926-935
116. Ruggero D., and Pandolfi P.P. Does the ribosome translate cancer?. Nat. Rev. Cancer 3 (2003) 179-192
117. Lazaris-Karatzas A., Montine K.S., and Sonenberg N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′cap. Nature 345 (1990) 544-547
118. De Benedetti A., and Graff J.R. eIF-4E expression and its role in malignancies and metastases. Oncogene 23 (2004) 3189-3199
119. Ruggero D., Montanaro L., Ma L., Xu W., Londei P., Cordon-Cardo C., and Pandolfi P.P. The translation factor eIF-4E promotes tumor formation and cooperates with c-myc in lymphomagenesis. Nat. Med. 10 (2004) 484-486
120. Kim S.H., Forman A.P., Mathews M.B., and Gunnery S. Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR. Oncogene 19 (2000) 3086-3094
121. Balachandran S., and Barber G.N. Defective translational control facilitates vesicular stomatitis virus oncolysis. Cancer Cell 5 (2004) 51-65
122. Tuhackova Z., Sloncova E., Hlavacek J., Sovova V., and Velek J. Activity of glycogen synthase kinase-3beta is down-regulated during transient differentiation of human colon cancer HT-29 cells. Oncol. Rep. 6 (1999) 827-832
123. Vojtechova M., Sloncova E., Kucerova D., Jiricka J., Sovova V., and Tuhackova Z. Initiation factor eIF2B not p70 S6 kinase is involved in the activation of the PI-3K signalling pathway induced by the v-src oncogene. FEBS Lett. 543 (2003) 81-86
124. Myers M.P., Pass I., Batty I.H., Van der Kaay J., Stolarov J.P., Hemmings B.A., Wigler M.H., Downes C.P., and Tonks N.K. The lipid phosphatase activity of PTEN is critical for its tumor supressor function. Proc. Natl. Acad. Sci. USA 95 (1998) 13513-13518
125. Maehama T., and Dixon J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273 (1998) 13375-13378
126. Cantley L.C., and Neel B.G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. USA 96 (1999) 4240-4245
127. Li J., Yen C., Liaw D., Podsypanina K., Bose S., Wang S.I., Puc J., Miliaresis C., Rodgers L., McCombie R., Bigner S.H., Giovanella B.C., et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 275 (1997) 1943-1947
128. Liaw D., Marsh D.J., Li J., Dahia P.L., Wang S.I., Zheng Z., Bose S., Call K.M., Tsou H.C., Peacocke M., Eng C., and Parsons R. Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat. Genet. 16 (1997) 64-67
129. Manning B.D., Logsdon M.N., Lipovsky A.I., Abbott D., Kwiatkowski D.J., and Cantley L.C. Feedback inhibition of Akt signaling limits the growth of tumors lacking Tsc2. Genes Dev. 19 (2005) 1773-1778
130. Parrillo J.E. Pathogenetic mechanisms of septic shock. N. Engl. J. Med. 328 (1993) 1471-1478
131. Hotchkiss R.S., and Karl I.E. The pathophysiology and treatment of sepsis. N. Engl. J. Med. 348 (2003) 138-150
132. Vary T.C., Siegel J.H., Tall B.D., Morris J.G., and Smith J.A. Inhibition of skeletal muscle protein synthesis in septic intra-abdominal abscess. J. Trauma-Injury Infect. Crit. Care 28 (1988) 981-988
133. Vary T.C., and Kimball S.R. Sepsis-induced changes in protein synthesis: Differential effects on fast- and slow-twitch muscles. Am. J. Physiol. 262 (1992) C1513-C1519
134. Vary T.C., Jurasinski C.V., Karinch A.M., and Kimball S.R. Regulation of eukaryotic initiation factor-2 expression during sepsis. Am. J. Physiol. 266 (1994) E193-E201
135. Voisin L., Gray K., Flowers K.M., Kimball S.R., Jefferson L.S., and Vary T.C. Altered expression of eukaryotic initiation factor 2B in skeletal muscle during sepsis. Am. J. Physiol. 270 (1996) E43-E50
136. Vary T.C., Deiter G., and Kimball S.R. Phosphorylation of eukaryotic initiation factor eIF2Bepsilon in skeletal muscle during sepsis. Am. J. Physiol. 283 (2002) E1032-E1039
137. Jurasinski C.V., and Vary T.C. Insulin-like growth factor I accelerates protein synthesis in skeletal muscle during sepsis. Am. J. Physiol. 269 (1995) E977-E981
138. Vary T.C., Jefferson L.S., and Kimball S.R. Insulin fails to stimulate muscle protein synthesis in sepsis despite unimpaired signaling to 4E-BP1 and S6K1. Am. J. Physiol. 281 (2001) E1045-E1053
139. Jurasinski C.V., and Vary T.C. Insulin-like growth factor I accelerates protein synthesis in skeletal muscle during sepsis. Am. J. Physiol. 269 (1995) E977-E981
140. Lang C.H., Fan J., Cooney R., and Vary T.C. IL-1 receptor antagonist attenuates sepsis-induced alterations in the IGF system and protein synthesis. Am. J. Physiol. 270 (1996) E430-E437
141. Svanberg E., Frost R.A., Lang C.H., Isgaard J., Jefferson L.S., Kimball S.R., and Vary T.C. IGF-I/IGFBP-3 binary complex modulates sepsis-induced inhibition of protein synthesis in skeletal muscle. Am. J. Physiol. 279 (2000) E1145-E1158
142. Vary T.C., Voisin L., and Cooney R.N. Regulation of peptide-chain initiation in muscle during sepsis by interleukin-1 receptor antagonist. Am. J. Physiol. 271 (1996) E513-E520
143. Cooney R., Kimball S.R., Eckman R., Maish III G., Shumate M., and Vary T.C. TNF-binding protein ameliorates inhibition of skeletal muscle protein synthesis during sepsis. Am. J. Physiol. 276 (1999) E611-E619
144. van der Knaap M.S., Smit L.M., Barth P.G., Catsman-Berrevoets C.E., Brouwer O.F., Begeer J.H., de Coo I.F., and Valk J. Magnetic resonance imaging in classification of congenital muscular dystrophies with brain abnormalities. Ann. Neurol. 42 (1997) 50-59
145. van der Knaap M.S., Kamphorst W., Barth P.G., Kraaijeveld C.L., Gut E., and Valk J. Phenotypic variation in leukoencephalopathy with vanishing white matter. Neurology 51 (1998) 540-547
146. Leegwater P.A., Konst A.A., Kuyt B., Sandkuijl L.A., Naidu S., Oudejans C.B., Schutgens R.B., Pronk J.C., and van der Knaap M.S. The gene for leukoencephalopathy with vanishing white matter is located on chromosome 3q27. Am. J. Hum. Genet. 65 (1999) 728-734
147. Leegwater P.A., Vermeulen G., Konst A.A., Naidu S., Mulders J., Visser A., Kersbergen P., Mobach D., Fonds D., van Berkel C.G., Lemmers R.J., Frants R.R., et al. Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter. Nat. Genet. 29 (2001) 383-388
148. van der Knaap M.S. Magnetic resonance in childhood white-matter disorders. Dev. Med. Child Neurol. 43 (2001) 705-712
149. Abbott C.M., and Proud C.G. Translation factors: In sickness and in health. Trends Biochem. Sci. 29 (2004) 25-31
150. Fogli A., and Boespflug-Tanguy O. The large spectrum of eIF2B-related diseases. Biochem. Soc. Trans. 34 (2006) 22-29
151. Pavitt G.D. eIF2B, a mediator of general and gene-specific translational control. Nucl. Gene Express 33 (2005) 1487-1492
152. Fogli A., Dionisi-Vici C., Deodato F., Bartuli A., Boespflug-Tanguy O., and Bertini E. A severe variant of childhood ataxia with central hypomyelination/vanishing white matter leukoencephalopathy related to EIF21B5 mutation. Neurology 59 (2002) 1966-1968
153. Fogli A., Wong K., Eymard-Pierre E., Wenger J., Bouffard J.P., Goldin E., Black D.N., Boespflug-Tanguy O., and Schiffmann R. Cree leukoencephalopathy and CACH/VWM disease are allelic at the EIF2B5 locus. Ann. Neurol. 52 (2002) 506-510
154. Richardson J.P., Mohammad S.S., and Pavitt G.D. Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity. Mol. Cell. Biol. 24 (2004) 2352-2363
155. Li W., Wang X., van der Knaap M.S., and Proud C.G. Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways. Mol. Cell. Biol. 24 (2004) 3295-3306
156. Fogli A., Schiffmann R., Hugendubler L., Combes P., Bertini E., Rodriguez D., Kimball S.R., and Boespflug-Tanguy O. Decreased guanine nucleotide exchange factor activity in eIF2B-mutated patients. Eur. J. Hum. Genet. 12 (2004) 561-566
157. Hinnebusch A.G. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. In: Sonenberg N., Hershey, J.W.B., and Mathews M.B. (Eds). "Translational Control" (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 185-243
158. Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., and Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6 (2000) 1099-1108
159. Kantor L., Harding H.P., Ron D., Schiffmann R., Kaneski C.R., Kimball S.R., and Elroy-Stein O. Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients. Hum. Genet. 118 (2005) 99-106
160. van der Voorn J.P., van Kollenburg B., Bertrand G., Van Haren K., Scheper G.C., Powers J.M., and van der Knaap M.S. The unfolded protein response in vanishing white matter disease. J. Neuropathol. Exp. Neurol. 64 (2005) 770-775
161. Inamura N., Nawa H., and Takei N. Developmental changes of eukaryotic initiation factor 2B subunits in rat hippocampus. Neurosci. Lett. 346 (2003) 117-119
162. Dietrich J., Lacagnina M., Gass D., Richfield E., Mayer-Proschel M., Noble M., Torres C., and Proschel C. EIF2B5 mutations compromise GFAP+ astrocyte generation in vanishing white matter leukodystrophy. Nat. Med. 11 (2005) 277-283