Chapter 3 Ribosomal Protein S6 Kinase. From TOP mRNAs to Cell Size

Progress in Molecular Biology and Translational Science

Volumn 90, Issue C, 2009, Pages 109-153

  Meyuhas, Oded ^a   Dreazen, Avigail ^a  

^a HEBREW UNIVERSITY   (Israel)

Author keywords

Cell size; Energy balance; Glucose homeostasis; Growth control; Insulin resistance; Mitogenic stimulation; mTOR; S6 phosphorylation; Translational control

Indexed keywords

S6 KINASE;

ANIMAL; CELL SIZE; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN SYNTHESIS; REVIEW; TERMINAL OLIGOPYRIMIDINE TRACT;

ANIMALS; BASE SEQUENCE; CELL SIZE; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; RIBOSOMAL PROTEIN S6 KINASES; RNA 5' TERMINAL OLIGOPYRIMIDINE SEQUENCE; SUBSTRATE SPECIFICITY;

EID: 77957075353     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1877-1173(09)90003-5     Document Type: Review

References (231)

1. Erikson E., and Maller J. A protein kinase from Xenopus eggs specific for ribosomal protein S6. Proc Natl Acad Sci USA 82 (1985) 742-746
2. Blenis J., Kuo C.J., and Erikson R.L. Identification of a ribosomal protein S6 kinase regulated by transformation and growth-promoting stimuli. J Biol Chem 262 (1987) 14373-14376
3. Jenö P., Ballou L., Novak-Hofer I., and Thomas G. Identification and characterization of a mitogenic-activated S6 kinase. Proc Natl Acad Sci USA 85 (1988) 406-410
4. Ballou L., Luther H., and Thomas G. MAP2 kinase and 70K S6 kinase lie on distinct signalling pathways. Nature 349 (1991) 348-350
5. Chung J., Kuo C.J., Crabtree G.R., and Blenis J. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 kinases. Cell 69 (1992) 1227-1236
6. Martin K.A., Schalm S.S., Romanelli A., Keon K.L., and Blenis J. Ribosomal S6 kinase 2 inhibition by a potent C-terminal repressor domain is relieved by mitogen-activated protein-extracellular signal-regulated kinase kinase-regulated phosphorylation. J Biol Chem 276 (2001) 7892-7898
7. Rossi R., Pester J.M., McDowell M., Soza S., Montecucco A., and Lee-Fruman K.K. Identification of S6K2 as a centrosome-located kinase. FEBS Lett 581 (2007) 4058-4064
8. Karni R., de Stanchina E., Lowe S.W., Sinha R., Mu D., and Krainer A.R. The gene encoding the splicing factor SF2/ASF is a proto-oncogene. Nat Struct Mol Biol 14 (2007) 185-193
9. Cantrell D.A. Phosphoinositide 3-kinase signalling pathways. J Cell Sci 114 (2001) 1439-1445
10. Leslie N.R., and Downes C.P. PTEN: the down side of PI 3-kinase signalling. Cell Signal 14 (2002) 285-295
11. Brazil D.P., and Hemmings B.A. Ten years of protein kinase B signalling: a hard Akt to follow. Trends Biochem Sci 26 (2001) 657-664
12. Belham C., Wu S., and Avruch J. Intracellular signalling: PDK1-a kinase at the hub of things. Curr Biol 9 (1999) R93-R96
13. Alessi D., Kozlowski M., Weng Q., Morrice N., and Avruch J. 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr Biol 8 (1998) 69-81
14. Balendran A., Currie R., Armstrong C.G., Avruch J., and Alessi D.R. Evidence that 3-phosphoinositide-dependent protein kinase-1 mediates phosphorylation of p70 S6 kinase in vivo at Thr-412 as well as Thr-252. J Biol Chem 274 (1999) 37400-37406
15. Huang J., and Manning B.D. The TSC1-TSC2 complex: a molecular switchboard controlling cell growth. Biochem J 412 (2008) 179-190
16. Avruch J., Hara K., Lin Y., Liu M., Long X., Ortiz-Vega S., et al. Insulin and amino-acid regulation of mTOR signaling and kinase activity through the Rheb GTPase. Oncogene 25 (2006) 6361-6372
17. Chen J., Zheng X.F., Brown E.J., and Schreiber S.L. Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue. Proc Natl Acad Sci USA 92 (1995) 4947-4951
18. Polak P., and Hall M.N. mTOR and the control of whole body metabolism. Curr Opin Cell Biol 21 (2009) 209-218
19. Dunlop E.A., and Tee A.R. Mammalian target of rapamycin complex 1: signalling inputs, substrates and feedback mechanisms. Cell Signal 21 (2009) 827-835
20. Bai X., Ma D., Liu A., Shen X., Wang Q.J., Liu Y., et al. Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38. Science 318 (2007) 977-980
21. Wang X., Fonseca B.D., Tang H., Liu R., Elia A., Clemens M.J., et al. Re-evaluating the roles of proposed modulators of mammalian target of rapamycin complex 1 (mTORC1) signaling. J Biol Chem 283 (2008) 30482-30492
22. Weng Q., Kozlowski M., Belham C., Zhang A., Comb M., and Avruch J. Regulation of the p70 S6 kinase by phosphorylation in vivo. Analysis using site-specific anti-phosphopeptide antibodies. J Biol Chem 273 (1998) 16621-16629
23. Gingras A.C., Raught B., and Sonenberg N. Regulation of translation initiation by FRAP/mTOR. Genes Dev 15 (2001) 807-826
24. Woo S.Y., Kim D.H., Jun C.B., Kim Y.M., Haar E.V., Lee S.I., et al. PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling. J Biol Chem 282 (2007) 25604-25612
25. Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., et al. Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but Not S6K1. Dev Cell 11 (2006) 859-871
26. Sarbassov D.D., Ali S.M., Sengupta S., Sheen J.H., Hsu P.P., Bagley A.F., et al. Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB. Mol Cell 22 (2006) 159-168
27. Fingar D.C., and Blenis J. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 23 (2004) 3151-3171
28. Fingar D.C., Salama S., Tsou C., Harlow E., and Blenis J. Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. Genes Dev 16 (2002) 1472-1487
29. Kleijn M., and Proud C.G. Glucose and amino acids modulate translation factor activation by growth factors in PC12 cells. Biochem J 347 (2000) 399-406
30. Rudkin B.B., Lazarovici P., Levi B.Z., Abe Y., Fujita K., and Guroff G. Cell cycle-specific action of nerve growth factor in PC12 cells: differentiation without proliferation. EMBO J 8 (1989) 3319-3325
31. McMullen J.R., and Izumu S. Mechanisms controlling heart growth in mammals. In: Hall M.N., Raff M., and Thomas G. (Eds). Cell growth: control of cell size (2004), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 549-603
32. Shioi T., Kang P.M., Douglas P.S., Hampe J., Yballe C.M., Lawitts J., et al. The conserved phosphoinositide 3-kinase pathway determines heart size in mice. EMBO J 19 (2000) 2537-2548
33. McMullen J.R., Shioi T., Zhang L., Tarnavski O., Sherwood M.C., Dorfman A.L., et al. Deletion of ribosomal S6 kinases does not attenuate pathological, physiological, or insulin-like growth factor 1 receptor-phosphoinositide 3-kinase-induced cardiac hypertrophy. Mol Cell Biol 24 (2004) 6231-6240
34. Vaughan Jr. M.H., Pawlowski P.J., and Forchhammer J. Regulation of protein synthesis initiation in HeLa cells deprived of single essential amino acids. Proc Natl Acad Sci USA 68 (1971) 2057-2061
35. Hara K., Yonezawa K., Weng Q.-P., Kozlowski M.T., Belham C., and Avruch J. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J Biol Chem 273 (1998) 14484-14494
36. Avruch J., Long X., Ortiz-Vega S., Rapley J., Papageorgiou A., and Dai N. Amino acid regulation of TOR complex 1. Am J Physiol Endocrinol Metab 296 (2009) E592-E602
37. Kimball S.R., and Jefferson L.S. Role of amino acids in the translational control of protein synthesis in mammals. Semin Cell Dev Biol 16 (2005) 21-27
38. Proud C.G. Amino acids and mTOR signalling in anabolic function. Biochem Soc Trans 35 (2007) 1187-1190
39. Holz M.K., Ballif B.A., Gygi S.P., and Blenis J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123 (2005) 569-580
40. Herbert T.P., and Proud C.G. Regulation of translation elongation and the cotranslational protein targeting pathway. In: Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational control in biology and medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 601-624
41. Wang X., Campbell L.E., Miller C.M., and Proud C.G. Amino acid availability regulates p70 S6 kinase and multiple translation factors. Biochem J 334 (1998) 261-267
42. Tang H., Hornstein E., Stolovich M., Levy G., Livingstone M., Templeton D.J., et al. Amino acid-induced translation of TOP mRNAs is fully dependent on PI3-kinase-mediated signaling, is partially inhibited by rapamycin, and is independent of S6K1 and rpS6 phosphorylation. Mol Cell Biol 21 (2001) 8671-8683
43. Manning B.D., and Cantley L.C. AKT/PKB signaling: navigating downstream. Cell 129 (2007) 1261-1274
44. Yanagida O., Kanai Y., Chairoungdua A., Kim D.K., Segawa H., Nii T., et al. Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines. Biochim Biophys Acta 1514 (2001) 291-302
45. Nicklin P., Bergman P., Zhang B., Triantafellow E., Wang H., Nyfeler B., et al. Bidirectional transport of amino acids regulates mTOR and autophagy. Cell 136 (2009) 521-534
46. Kim E., Goraksha-Hicks P., Li L., Neufeld T.P., and Guan K.L. Regulation of TORC1 by Rag GTPases in nutrient response. Nat Cell Biol 10 (2008) 935-945
47. Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., Bar-Peled L., et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320 (2008) 1496-1501
48. Sun Y., Fang Y., Yoon M.S., Zhang C., Roccio M., Zwartkruis F.J., et al. Phospholipase D1 is an effector of Rheb in the mTOR pathway. Proc Natl Acad Sci USA 105 (2008) 8286-8291
49. Byfield M.P., Murray J.T., and Backer J.M. hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J Biol Chem 280 (2005) 33076-33082
50. Nobukuni T., Joaquin M., Roccio M., Dann S.G., Kim S.Y., Gulati P., et al. Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase. Proc Natl Acad Sci USA 102 (2005) 14238-14243
51. Tassa A., Roux M.P., Attaix D., and Bechet D.M. Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem J 376 (2003) 577-586
52. Juhasz G., Hill J.H., Yan Y., Sass M., Baehrecke E.H., Backer J.M., et al. The class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila. J Cell Biol 181 (2008) 655-666
53. Maehama T., Tanaka M., Nishina H., Murakami M., Kanaho Y., and Hanada K. RalA functions as an indispensable signal mediator for the nutrient-sensing system. J Biol Chem 283 (2008) 35053-35059
54. Findlay G.M., Yan L., Procter J., Mieulet V., and Lamb R.F. A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of mTOR signalling. Biochem J 403 (2007) 13-20
55. Dennis P.B., Jaeschke A., Saitoh M., Fowler B., Kozma S.C., and Thomas G. Mammalian TOR: a homeostatic ATP sensor. Science 294 (2001) 1102-1105
56. Inoki K., Zhu T., and Guan K.L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115 (2003) 577-590
57. Kim D.H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110 (2002) 163-175
58. Towler M.C., and Hardie D.G. AMP-activated protein kinase in metabolic control and insulin signaling. Circ Res 100 (2007) 328-341
59. Corradetti M.N., Inoki K., Bardeesy N., DePinho R.A., and Guan K.L. Regulation of the TSC pathway by LKB1: evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev 18 (2004) 1533-1538
60. Shaw R.J., Bardeesy N., Manning B.D., Lopez L., Kosmatka M., DePinho R.A., et al. The LKB1 tumor suppressor negatively regulates mTOR signaling. Cancer Cell 6 (2004) 91-99
61. Bolster D.R., Crozier S.J., Kimball S.R., and Jefferson L.S. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J Biol Chem 277 (2002) 23977-23980
62. Kimura N., Tokunaga C., Dalal S., Richardson C., Yoshino K., Hara K., et al. A possible linkage between AMP-activated protein kinase (AMPK) and mammalian target of rapamycin (mTOR) signalling pathway. Genes Cells 8 (2003) 65-79
63. Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A., Vasquez D.S., et al. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol Cell 30 (2008) 214-226
64. Semenza G.L. Regulation of oxygen homeostasis by hypoxia-inducible factor 1. Physiology (Bethesda) 24 (2009) 97-106
65. Shoshani T., Faerman A., Mett I., Zelin E., Tenne T., Gorodin S.Y.M., et al. Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis. Mol Cell Biol 22 (2002) 2283-2293
66. DeYoung M.P., Horak P., Sofer A., Sgroi D., and Ellisen L.W. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev 22 (2008) 239-251
67. Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E., et al. Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex. Genes Dev 18 (2004) 2893-2904
68. Liu L., Cash T.P., Jones R.G., Keith B., Thompson C.B., and Simon M.C. Hypoxia-induced energy stress regulates mRNA translation and cell growth. Mol Cell 21 (2006) 521-531
69. Burg M.B., Ferraris J.D., and Dmitrieva N.I. Cellular response to hyperosmotic stresses. Physiol Rev 87 (2007) 1441-1474
70. Parrott L.A., and Templeton D.J. Osmotic stress inhibits p70/85 S6 kinase through activation of a protein phosphatase. J Biol Chem 274 (1999) 24731-24736
71. Richter J.D., and Klann E. Making synaptic plasticity and memory last: mechanisms of translational regulation. Genes Dev 23 (2009) 1-11
72. Costa-Mattioli M., Sossin W.S., Klann E., and Sonenberg N. Translational control of long-lasting synaptic plasticity and memory. Neuron 61 (2009) 10-26
73. Tsokas P., Grace E.A., Chan P., Ma T., Sealfon S.C., Iyengar R., et al. Local protein synthesis mediates a rapid increase in dendritic elongation factor 1A after induction of late long-term potentiation. J Neurosci 25 (2005) 5833-5843
74. Lenz G., and Avruch J. Glutamatergic regulation of the p70S6 kinase in primary mouse neurons. J Biol Chem 280 (2005) 38121-38124
75. Meyuhas O. Physiological roles of ribosomal protein S6: one of its kind. Int Rev Cell Mol Biol 268 (2008) 1-37
76. Krieg J., Hofsteenge J., and Thomas G. Identification of the 40 S ribosomal protein S6 phosphorylation sites induced by cycloheximide. J Biol Chem 263 (1988) 11473-11477
77. Flotow H., and Thomas G. Substrate recognition determinants of the mitogen-activated 70K S6 kinase from rat liver. J Biol Chem 267 (1992) 3074-3078
78. Wettenhall R.E., Erikson E., and Maller J.L. Ordered multisite phosphorylation of Xenopus ribosomal protein S6 by S6 kinase II. J Biol Chem 267 (1992) 9021-9027
79. -/- mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway. Mol Cell Biol 24 (2004) 3112-3124
80. Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., et al. RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation. J Biol Chem 282 (2007) 14056-14064
81. Moore C.E., Xie J., Gomez E., and Herbert T.P. Identification of cAMP-dependent kinase as a third in vivo ribosomal protein S6 kinase in pancreatic beta-cells. J Mol Biol 389 (2009) 480-494
82. Ruvinsky I., Sharon N., Lerer T., Cohen H., Stolovich-Rain M., Nir T., et al. Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis. Genes Dev 19 (2005) 2199-2211
83. Methot N., Song M.S., and Sonenberg N. A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol Cell Biol 16 (1996) 5328-5334
84. Rogers G.W.J., Richter N.J., Lima W.F., and Merrick W.C. Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J Biol Chem 276 (2001) 30914-30922
85. Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D., Mayeur G.L., et al. Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases. EMBO J 23 (2004) 1761-1769
86. Mieulet V., Roceri M., Espeillac C., Sotiropoulos A., Ohanna M., Oorschot V., et al. S6 kinase inactivation impairs growth and translational target phosphorylation in muscle cells maintaining proper regulation of protein turnover. Am J Physiol Cell Physiol 293 (2007) C712-C722
87. Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., et al. The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity. EMBO J 25 (2006) 2781-2791
88. van Gorp A.G., van der Vos K.E., Brenkman A.B., Bremer A., van den Broek N., Zwartkruis F., et al. AGC kinases regulate phosphorylation and activation of eukaryotic translation initiation factor 4B. Oncogene 28 (2009) 95-106
89. Garber K.B., Visootsak J., and Warren S.T. Fragile X syndrome. Eur J Hum Genet 16 (2008) 666-672
90. Bassell G.J., and Warren S.T. Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function. Neuron 60 (2008) 201-214
91. Brown V., Jin P., Ceman S., Darnell J.C., O'Donnell W.T., Tenenbaum S.A., et al. Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome. Cell 107 (2001) 477-487
92. Narayanan U., Nalavadi V., Nakamoto M., Thomas G., Ceman S., Bassell G.J., et al. S6K1 phosphorylates and regulates fragile X mental retardation protein (FMRP) with the neuronal protein synthesis-dependent mammalian target of rapamycin (mTOR) signaling cascade. J Biol Chem 283 (2008) 18478-18482
93. LaRonde-LeBlanc N., Santhanam A.N., Baker A.R., Wlodawer A., and Colburn N.H. Structural basis for inhibition of translation by the tumor suppressor Pdcd4. Mol Cell Biol 27 (2007) 147-156
94. Suzuki C., Garces R.G., Edmonds K.A., Hiller S., Hyberts S.G., Marintchev A., et al. PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains. Proc Natl Acad Sci USA 105 (2008) 3274-3279
95. Dorrello N.V., Peschiaroli A., Guardavaccaro D., Colburn N.H., Sherman N.E., and Pagano M. S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth. Science 314 (2006) 467-471
96. Wang X., Li W., Williams M., Terada N., Alessi D.R., and Proud C.G. Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase. EMBO J 20 (2001) 4370-4379
97. Chiang G.G., and Abraham R.T. Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase. J Biol Chem 280 (2005) 25485-25490
98. Holz M.K., and Blenis J. Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase. J Biol Chem 280 (2005) 26089-26093
99. Harada H., Andersen J., Mann M., Terada N., and Korsmeyer S. p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD. Proc Natl Acad Sci USA 98 (2001) 9666-9670
100. Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., et al. S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling. Mol Cell 28 (2007) 28-40
101. Yamnik R.L., Digilova A., Davis D.C., Brodt Z.N., Murphy C.J., and Holz M.K. S6 kinase 1 regulates estrogen receptor alpha in control of breast cancer cell proliferation. J Biol Chem 284 (2009) 6361-6369
102. de Groot R., Ballou L.M., and Sassone-Corsi P. Positive regulation of the cAMP-responsive activator CREM by the p70 S6 kinase: an alternative route to mitogen-induced gene expression. Cell 79 (1994) 81-91
103. Richardson C.J., Broenstrup M., Fingar D.C., Julich K., Ballif B.A., Gygi S., et al. SKAR is a specific target of S6 kinase 1 in cell growth control. Curr Biol 14 (2004) 1540-1549
104. Ma X.M., Yoon S.O., Richardson C.J., Julich K., and Blenis J. SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs. Cell 133 (2008) 303-313
105. Maquat L.E. Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics. Nat Rev Mol Cell Biol 5 (2004) 89-99
106. Wilson K.F., Wu W.J., and Cerione R.A. Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase target, the nuclear cap-binding complex. J Biol Chem 275 (2000) 37307-37310
107. Harrington L.S., Findlay G.M., Gray A., Tolkacheva T., Wigfield S., Rebholz H., et al. The TSC1-2 tumor suppressor controls insulin-PI3K signaling via regulation of IRS proteins. J Cell Biol 166 (2004) 213-223
108. 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
109. Um S.H., Frigerio F., Watanabe M., Picard F., Joaquin M., Sticker M., et al. Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 431 (2004) 200-205
110. Tremblay F., Brule S., Hee Um S., Li Y., Masuda K., Roden M., et al. Identification of IRS-1 Ser-1101 as a target of S6K1 in nutrient- and obesity-induced insulin resistance. Proc Natl Acad Sci USA 104 (2007) 14056-14061
111. Zhang J., Gao Z., Yin J., Quon M.J., and Ye J. S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-(alpha) signaling through IKK2. J Biol Chem 283 (2008) 35375-35382
112. Nygard O., and Nika H. Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes. EMBO J 1 (1982) 357-362
113. Jefferies H.B.J., and Thomas G. Ribosomal protein S6 phosphorylation and signal transduction. In: Hershey J.W.B., Mathews M.B., and Sonenberg N. (Eds). Translational control (1996), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 389-409
114. Jefferies H.B.J., Fumagalli S., Dennis P.B., Reinhard C., Pearson R.B., and Thomas G. Rapamycin suppresses 5′TOP mRNA translation through inhibition of p70s6k. EMBO J 16 (1997) 3693-3704
115. Perry R.P. The architecture of mammalian ribosomal protein promoters. BMC Evol Biol 5 (2005) 15
116. Juven-Gershon T., Hsu J.Y., Theisen J.W., and Kadonaga J.T. The RNA polymerase II core promoter-the gateway to transcription. Curr Opin Cell Biol 20 (2008) 253-259
117. Schibler U., Kelley D.E., and Perry R.P. Comparison of methylated sequences in messenger RNA and heterogeneous nuclear RNA from mouse L cells. J Mol Biol 115 (1977) 695-714
118. Avni D., Shama S., Loreni F., and Meyuhas O. Vertebrate mRNAs with a 5′-terminal pyrimidine tract are candidates for translational repression in quiescent cells: characterization of the translational cis-regulatory element. Mol Cell Biol 14 (1994) 3822-3833
119. Levy S., Avni D., Hariharan N., Perry R.P., and Meyuhas O. Oligopyrimidine tract at the 5′ end of mammalian ribosomal protein mRNAs is required for their translational control. Proc Natl Acad Sci USA 88 (1991) 3319-3323
120. Avni D., Biberman Y., and Meyuhas O. The 5′ terminal oligopyrimidine tract confers translational control on TOP mRNAs in a cell type-and sequence context-dependent manner. Nucleic Acids Res 25 (1997) 995-1001
121. Hornstein E., Git A., Braunstein I., Avni D., and Meyuhas O. The expression of poly (A)-binding protein gene is translationally regulated in a growth dependent fashion through a 5′-terminal oligopyrimidine tract motif. J Biol Chem 274 (1999) 1708-1714
122. Ledda M., Di Croce M., Bedini B., Wannenes F., Corvaro M., Boyl P.P., et al. Effect of 3′UTR length on the translational regulation of 5′-terminal oligopyrimidine mRNAs. Gene 344 (2005) 213-220
123. Geyer P.K., Meyuhas O., Perry R.P., and Johnson L.F. Regulation of ribosomal protein mRNA content and translation in growth-stimulated mouse fibroblasts. Mol Cell Biol 2 (1982) 685-693
124. Yamashita R., Suzuki Y., Takeuchi N., Wakaguri H., Ueda T., Sugano S., et al. Comprehensive detection of human terminal oligo-pyrimidine (TOP) genes and analysis of their characteristics. Nucleic Acids Res 36 (2008) 3707-3715
125. Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., et al. The human ribosomal protein genes: sequencing and comparative analysis of 73 genes. Genome Res 12 (2002) 379-390
126. Warner J.R., and McIntosh K.B. How common are extraribosomal functions of ribosomal proteins?. Mol Cell 34 (2009) 3-11
127. Olson M.O., Orrick L.R., Jones C., and Busch H. Phosphorylation of acid-soluble nucleolar proteins of Novikoff hepatoma ascites cells in vivo. J Biol Chem 249 (1974) 2823-2827
128. Okuwaki M. The structure and functions of NPM1/nucleophsmin/B23, a multifunctional nucleolar acidic protein. J Biochem 143 (2008) 441-448
129. Grisendi S., Bernardi R., Rossi M., Cheng K., Khandker L., Manova K., et al. Role of nucleophosmin in embryonic development and tumorigenesis. Nature 437 (2005) 147-153
130. Colombo E., Bonetti P., Lazzerini Denchi E., Martinelli P., Zamponi R., Marine J.C., et al. Nucleophosmin is required for DNA integrity and p19Arf protein stability. Mol Cell Biol 25 (2005) 8874-8886
131. Borer R.A., Lehner C.F., Eppenberger H.M., and Nigg E.A. Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56 (1989) 379-390
132. Dumbar T.S., Gentry G.A., and Olson M.O. Interaction of nucleolar phosphoprotein B23 with nucleic acids. Biochemistry 28 (1989) 9495-9501
133. Savkur R.S., and Olson M.O. Preferential cleavage in pre-ribosomal RNA by protein B23 endoribonuclease. Nucleic Acids Res 26 (1998) 4508-4515
134. Maggi Jr. L.B., Kuchenruether M., Dadey D.Y., Schwope R.M., Grisendi S., Townsend R.R., et al. Nucleophosmin serves as a rate-limiting nuclear export chaperone for the mammalian ribosome. Mol Cell Biol 28 (2008) 7050-7065
135. Zong Q., Schummer M., Hood L., and Morris D. Messenger RNA translation state: the second dimension of high-throughput expression screening. Proc Natl Acad Sci USA 96 (1999) 10632-10636
136. Pestova T.V., Lorsch J.R., and Hellen C.U.T. The mechanism of translation initiation in eukaryotes. In: Methews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational control in biology and medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 87-128
137. Iadevaia V., Caldarola S., Tino E., Amaldi F., and Loreni F. All translation elongation factors and the e, f, and h subunits of translation initiation factor 3 are encoded by 5′-terminal oligopyrimidine (TOP) mRNAs. RNA 14 (2008) 1730-1736
138. Kahvejian A., Svitkin Y.V., Sukarieh R., M'Boutchou M.N., and Sonenberg N. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev 19 (2005) 104-113
139. Sachs A. Physical and functional interactions between the mRNA cap structure and the poly(A) tail. 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 447-465
140. Gorgoni B., and Gray N.K. The roles of cytoplasmic poly(A)-binding proteins in regulating gene expression: a developmental perspective. Brief Funct Genomic Proteomic 3 (2004) 125-141
141. Guillemot F., Billault A., and Auffray C. Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex. Proc Natl Acad Sci USA 86 (1989) 4594-4598
142. Mochly-Rosen D., Khaner H., and Lopez J. Identification of intracellular receptor proteins for activated protein kinase C. Proc Natl Acad Sci USA 88 (1991) 3997-4000
143. Regmi S., Rothberg K.G., Hubbard J.G., and Ruben L. The RACK1 signal anchor protein from Trypanosoma brucei associates with eukaryotic elongation factor 1A: a role for translational control in cytokinesis. Mol Microbiol 70 (2008) 724-745
144. Nilsson J., Sengupta J., Frank J., and Nissen P. Regulation of eukaryotic translation by the RACK1 protein: a platform for signalling molecules on the ribosome. EMBO Rep 5 (2004) 1137-1141
145. Yu Y., Ji H., Doudna J.A., and Leary J.A. Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes. Protein Sci 14 (2005) 1438-1446
146. Sengupta J., Nilsson J., Gursky R., Spahn C.M., Nissen P., and Frank J. Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM. Nat Struct Mol Biol 11 (2004) 957-962
147. Link A.J., Eng J., Schieltz D.M., Carmack E., Mize G.J., Morris D.R., et al. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol 17 (1999) 676-682
148. Inada T., Winstall E., Tarun Jr. S.Z., Yates III J.R., Schieltz D., and Sachs A.B. One-step affinity purification of the yeast ribosome and its associated proteins and mRNAs. RNA 8 (2002) 948-958
149. Ceci M., Gaviraghi C., Gorrini C., Sala L.A., Offenhauser N., Marchisio P.C., et al. Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly. Nature 426 (2003) 579-584
150. Shor B., Calaycay J., Rushbrook J., and McLeod M. Cpc2/RACK1 is a ribosome-associated protein that promotes efficient translation in Schizosaccharomyces pombe. J Biol Chem 278 (2003) 49119-49128
151. Loreni F., Iadevaia V., Tino E., Caldarola S., and Amaldi F. RACK1 mRNA translation is regulated via a rapamycin-sensitive pathway and coordinated with ribosomal protein synthesis. FEBS Lett 579 (2005) 5517-5520
152. Taylor D.J., Frank J., and Kinzy T.G. Structure and function of the eukaryotic ribosme and elongation factors. In: Methews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational control in biology and medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor 59-85
153. Thomas G., Thomas G., and Luther H. Transcriptional and translational control of cytoplasmic proteins after serum stimulation of quiescent Swiss 3T3 cells. Proc Natl Acad Sci USA 78 (1981) 5712-5716
154. Rao T.R., and Slobin L.I. Regulation of the utilization of mRNA for eucaryotic elongation factor Tu in Friend erythroleukemia cells. Mol Cell Biol 7 (1987) 687-697
155. Gross B., Gaestel M., Bohm H., and Bielka H. cDNA sequence coding for a translationally controlled human tumor protein. Nucleic Acids Res 17 (1989) 8367
156. Yenofsky R., Bergman I., and Brawerman G. Messenger RNA species partially in a repressed state in mouse sarcoma ascites cells. Proc Natl Acad Sci USA 79 (1982) 5876-5880
157. Yenofsky R., Careghini S., Krowczynska A., and Brawerman G. Regulation of mRNA utilization in mouse erythroleukemia cells induced to differentiate by exposure to dimethyl sulfoxide. Mol Cell Biol 3 (1983) 1197-1203
158. Cans C., Passer B.J., Shalak V., Nancy-Portebois V., Crible V., Amzallag N., et al. Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A. Proc Natl Acad Sci USA 100 (2003) 13892-13897
159. MacDonald S.M., Rafnar T., Langdon J., and Lichtenstein L.M. Molecular identification of an IgE-dependent histamine-releasing factor. Science 269 (1995) 688-690
160. Gachet Y., Tournier S., Lee M., Lazaris-Karatzas A., Poulton T., and Bommer U. The growth-related, translationally controlled protein P23 has properties of a tubulin binding protein and associates transiently with microtubules during the cell cycle. J Cell Sci 112 (1999) 1257-1271
161. Telerman A., and Amson R. The molecular programme of tumour reversion: the steps beyond malignant transformation. Nat Rev Cancer 9 (2009) 206-216
162. Li F., Zhang D., and Fujise K. Characterization of fortilin, a novel antiapoptotic protein. J Biol Chem 276 (2001) 47542-47549
163. Chen S.H., Wu P.S., Chou C.H., Yan Y.T., Liu H., Weng S.Y., et al. A knockout mouse approach reveals that TCTP functions as an essential factor for cell proliferation and survival in a tissue- or cell type-specific manner. Mol Biol Cell 18 (2007) 2525-2532
164. Susini L., Besse S., Duflaut D., Lespagnol A., Beekman C., Fiucci G., et al. TCTP protects from apoptotic cell death by antagonizing bax function. Cell Death Differ 15 (2008) 1211-1220
165. Hsu Y.C., Chern J.J., Cai Y., Liu M., and Choi K.W. Drosophila TCTP is essential for growth and proliferation through regulation of dRheb GTPase. Nature 445 (2007) 785-788
166. Chitpatima S.T., Makrides S., Bandyopadhyay R., and Brawerman G. Nucleotide sequence for a major messenger RNA for a 21 kilodalton polypeptide that is under translational control in mouse tumor cells. Nucleic Acids Res 16 (1988) 2350
167. Pinol-Roma S., and Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355 (1992) 730-732
168. Mili S., Shu H.J., Zhao Y., and Pinol-Roma S. Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA. Mol Cell Biol 21 (2001) 7307-7319
169. Pollard A.J., Krainer A.R., Robson S.C., and Europe-Finner G.N. Alternative splicing of the adenylyl cyclase stimulatory G-protein G alpha(s) is regulated by SF2/ASF and heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) and involves the use of an unusual TG 3′-splice site. J Biol Chem 277 (2002) 15241-15251
170. Izaurralde E., Jarmolowski A., Beisel C., Mattaj I., Dreyfuss G., and Fischer U. A role for the M9 transport signal of hnRNP A1 in mRNA nuclear export. J Cell Biol 137 (1997) 27-35
171. Svitkin Y., Ovchinnikov L., Dreyfuss G., and Sonenberg N. General RNA binding proteins render translation cap dependent. EMBO J 15 (1996) 7147-7155
172. Bonnal S., Pileur F., Orsini C., Parker F., Pujol F., Prats A.C., et al. Heterogeneous nuclear ribonucleoprotein A1 is a novel internal ribosome entry site trans-acting factor that modulates alternative initiation of translation of the fibroblast growth factor 2 mRNA. J Biol Chem 280 (2005) 4144-4153
173. Lewis S.M., Veyrier A., Hosszu Ungureanu N., Bonnal S., Vagner S., and Holcik M. Subcellular relocalization of a trans-acting factor regulates XIAP IRES-dependent translation. Mol Biol Cell 18 (2007) 1302-1311
174. Hamilton B.J., Burns C.M., Nichols R.C., and Rigby W.F. Modulation of AUUUA response element binding by heterogeneous nuclear ribonucleoprotein A1 in human T lymphocytes. The roles of cytoplasmic location, transcription, and phosphorylation. J Biol Chem 272 (1997) 28732-28741
175. Guil S., and Caceres J.F. The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a. Nat Struct Mol Biol 14 (2007) 591-596
176. Camacho-Vanegas O., Weighardt F., Ghigna C., Amaldi F., Riva S., and Biamonti G. Growth-dependent and growth-independent translation of messengers for heterogeneous nuclear ribonucleoproteins. Nucleic Acids Res 25 (1997) 3950-3954
177. Shama S., Avni D., Frederickson R.M., Sonenberg N., and Meyuhas O. Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells. Gene Expression 4 (1995) 241-252
178. Stolovich M., Lerer T., Bolkier Y., Cohen H., and Meyuhas O. Lithium can relieve translational repression of TOP mRNAs elicited by various blocks along the cell cycle in a glycogen synthase kinase-3- and S6-kinase-independent manner. J Biol Chem 280 (2005) 5336-5342
179. Aloni R., Peleg D., and Meyuhas O. Selective translational control and nonspecific posttranscriptional regulation of ribosomal protein gene expression during development and regeneration of rat liver. Mol Cell Biol 12 (1992) 2203-2212
180. Hornstein E., Tang H., and Meyuhas O. Mitogenic and nutritional signals are transduced into translational efficiency of TOP mRNAs. Cold Spring Harb Symp Quant Biol 66 (2001) 477-484
181. Granneman S., and Tollervey D. Building ribosomes: even more expensive than expected?. Curr Biol 17 (2007) R415-R417
182. Lindstrom M.S., Deisenroth C., and Zhang Y. Putting a finger on growth surveillance: insight into MDM2 zinc finger-ribosomal protein interactions. Cell Cycle 6 (2007) 434-437
183. Fumagalli S., Di Cara A., Neb-Gulati A., Natt F., Schwemberger S., Hall J., et al. Absence of nucleolar disruption after impairment of 40S ribosome biogenesis reveals an rpL11-translation-dependent mechanism of p53 induction. Nat Cell Biol 11 (2009) 501-508
184. Greene L. Nerve growth factor prevents the death and stimulates the neuronal differentiation of clonal PC12 pheochromocytoma cells in serum-free medium. J Cell Biol 78 (1978) 747-755
185. Stolovich M., Tang H., Hornstein E., Levy G., Cohen R., Bae S.S., et al. Transduction of growth or mitogenic signals into translational activation of TOP mRNAs is fully reliant on the PI3-kinase-mediated pathway, but requires neither S6K1 nor rpS6 phosphorylation. Mol Cell Biol 22 (2002) 8101-8113
186. Proud C.G. Regulation of protein synthesis by insulin. Biochem Soc Trans 34 (2006) 213-216
187. Antonetti D.A., Kimball S.R., Horetsky R.L., and Jefferson L.S. Regulation of rDNA transcription by insulin in primary cultures of rat hepatocytes. J Biol Chem 268 (1993) 25277-25284
188. Patursky-Polischuk I., Stolovich-Rain M., Hausner-Hanochi M., Kasir J., Cybulski N., Avruch J., et al. The TSC-mTOR pathway mediates translational activation of TOP mRNAs by insulin largely in a raptor- or rictor-independent manner. Mol Cell Biol 29 (2009) 640-649
189. Copper G.T. Basic determinants of myocardial hypertrophy: a review of molecular mechanisms. Annu Rev Med 48 (1997) 13-23
190. Hannan R.D., Jenkins A., Jenkins A.K., and Brandenburger Y. Cardiac hypertrophy: a matter of translation. Clin Exp Pharmacol Physiol 30 (2003) 517-527
191. Tuxworth Jr. W.J., Shiraishi H., Moschella P.C., Yamane K., McDermott P.J., and Kuppuswamy D. Translational activation of 5′-TOP mRNA in pressure overload myocardium. Basic Res Cardiol 103 (2008) 41-53
192. Yamazaki T., Komuro I., Kudoh S., Zou Y., Shiojima I., Hiroi Y., et al. Endothelin-1 is involved in mechanical stress-induced cardiomyocyte hypertrophy. J Biol Chem 271 (1996) 3221-3228
193. Caldarola S., Amaldi F., Proud C.G., and Loreni F. Translational regulation of terminal oligopyrimidine mRNAs induced by serum and amino acids involves distinct signaling events. J Biol Chem 279 (2004) 13522-13531
194. Sutton M.A., and Schuman E.M. Dendritic protein synthesis, synaptic plasticity, and memory. Cell 127 (2006) 49-58
195. Tsokas P., Ma T., Iyengar R., Landau E.M., and Blitzer R.D. Mitogen-activated protein kinase upregulates the dendritic translation machinery in long-term potentiation by controlling the mammalian target of rapamycin pathway. J Neurosci 27 (2007) 5885-5894
196. Gobert D., Topolnik L., Azzi M., Huang L., Badeaux F., Desgroseillers L., et al. Forskolin induction of late-LTP and up-regulation of 5′ TOP mRNAs translation via mTOR, ERK, and PI3K in hippocampal pyramidal cells. J Neurochem 106 (2008) 1160-1174
197. Cantley L., and Neel B. 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
198. Bilanges B., Argonza-Barrett R., Kolesnichenko M., Skinner C., Nair M., Chen M., et al. Tuberous sclerosis complex proteins 1 and 2 control serum-dependent translation in a TOP-dependent and -independent manner. Mol Cell Biol 27 (2007) 5746-5764
199. Slobin L.I., and Rao M.N. Translational repression of EF-1α mRNA in vitro. Eur J Biochem 213 (1993) 919-926
200. Biberman Y., and Meyuhas O. TOP mRNAs are translationally inhibited by a titratable repressor in both wheat germ extract and reticulocyte lysate. FEBS Lett 456 (1999) 357-360
201. Kaspar R.L., Morris D.R., and White M. Control of ribosomal protein synthesi in eukaryotic cells. In: Ilan J. (Ed). Translational regulation of gene expression (1993), Plenum Press, New York 335-348
202. Pellizzoni L., Cardinali B., Lin-Marq N., Mercanti D., and Pierandrei-Amaldi P. A Xenopus laevis homologue of the La autoantigen binds the pyrimidine tract of the 5′UTR of ribosomal protein mRNAs in vitro: implication of a protein factor in complex formation. J Mol Biol 259 (1996) 904-915
203. Pellizzoni L., Lotti F., Maras B., and Pierandrei-Amaldi P. Cellular nucleic acid binding protein binds a conserved region of the 5′ UTR of Xenopus laevis ribosomal protein mRNAs. J Mol Biol 267 (1997) 264-275
204. Intine R.V., Tenenbaum S.A., Sakulich A.L., Keene J.D., and Maraia R.J. Differential phosphorylation and subcellular localization of La RNPs associated with precursor tRNAs and translation-related mRNAs. Mol Cell 12 (2003) 1301-1307
205. Brenet F., Socci N.D., Sonenberg N., and Holland E.C. Akt phosphorylation of La regulates specific mRNA translation in glial progenitors. Oncogene 28 (2009) 128-139
206. Markert A., Grimm M., Martinez J., Wiesner J., Meyerhans A., Meyuhas O., et al. The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes. EMBO Rep 9 (2008) 569-575
207. Caldarola S., De Stefano M.C., Amaldi F., and Loreni F. Synthesis and function of ribosomal proteins-fading models and new perspectives. FEBS J 276 (2009) 3199-3210
208. Orom U.A., Nielsen F.C., and Lund A.H. MicroRNA-10a binds the 5′UTR of ribosomal protein mRNAs and enhances their translation. Mol Cell 30 (2008) 460-471
209. Jefferies H.B.J., Reinhard C., Kozma S.C., and Thomas G. Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family. Proc Natl Acad Sci USA 91 (1994) 4441-4445
210. Barth-Baus D., Stratton C.A., Parrott L., Myerson H., Meyuhas O., Templeton D.J., et al. S6 phosphorylation-independent pathways regulate translation of 5′-terminal oligopyrimidine tract containing mRNAs in differentiating hematopoietic cells. Nucleic Acids Res 30 (2002) 1919-1928
211. Lee C.H., Inoki K., and Guan K.L. mTOR pathway as a target in tissue hypertrophy. Annu Rev Pharmacol Toxicol 47 (2007) 443-467
212. Montagne J., Stewart M.J., Stocker H., Hafen E., Kozma S.C., and Thomas G. Drosophila S6 kinase: a regulator of cell size. Science 285 (1999) 2126-2129
213. Shima H., Pende M., Chen Y., Fumagalli S., Thomas G., and Kozma S.C. Disruption of the p70s6k/p85s6k gene reveals a small mouse phenotype and a new functional S6 kinase. EMBO J 17 (1998) 6649-6659
214. Pende M., Kozma S.C., Jaquet M., Oorschot V., Burcelin R., Le Marchand-Brustel Y., et al. Hypoinsulinaemia, glucose intolerance and diminished beta-cell size in S6K1-deficient mice. Nature 408 (2000) 994-997
215. -/- skeletal muscle cells reveals distinct mTOR effectors for cell cycle and size control. Nat Cell Biol 7 (2005) 286-294
216. Ruvinsky I., Katz M., Dreazen A., Gielchinsky Y., Saada A., Freedman N., et al. Mice deficient in ribosomal protein S6 phosphorylation suffer from muscle weakness that reflects a growth defect and energy deficit. PLoS ONE 4 (2009) e5618
217. Lee C., Kim J.S., and Waldman T. PTEN gene targeting reveals a radiation-induced size checkpoint in human cancer cells. Cancer Res 64 (2004) 6906-6914
218. Kwon C.H., Zhu X., Zhang J., Knoop L.L., Tharp R., Smeyne R.J., et al. Pten regulates neuronal soma size: a mouse model of Lhermitte-Duclos disease. Nat Genet 29 (2001) 404-411
219. Backman S.A., Stambolic V., Suzuki A., Haight J., Elia A., Pretorius J., et al. Deletion of Pten in mouse brain causes seizures, ataxia and defects in soma size resembling Lhermitte-Duclos disease. Nat Genet 29 (2001) 396-403
220. Chalhoub N., Kozma S.C., and Baker S.J. S6k1 is not required for Pten-deficient neuronal hypertrophy. Brain Res 1100 (2006) 32-41
221. Tuttle R.L., Gill N.S., Pugh W., Lee J.P., Koeberlein B., Furth E.E., et al. Regulation of pancreatic β-cell growth and survival by the serine/threonine protein kinase Akt1/PKBα. Nat Med 7 (2001) 1133-1137
222. Bernal-Mizrachi E., Wen W., Stahlhut S., Welling C.M., and Permutt M.A. Islet β cell expression of constitutively active Akt1/PKBα induces striking hypertrophy, hyperplasia, and hyperinsulinemia. J Clin Invest 108 (2001) 1631-1638
223. Alliouachene S., Tuttle R.L., Boumard S., Lapointe T., Berissi S., Germain S., et al. Constitutively active Akt1 expression in mouse pancreas requires S6 kinase 1 for insulinoma formation. J Clin Invest 118 (2008) 3629-3638
224. Aguilar V., Alliouachene S., Sotiropoulos A., Sobering A., Athea Y., Djouadi F., et al. S6 kinase deletion suppresses muscle growth adaptations to nutrient availability by activating AMP kinase. Cell Metab 5 (2007) 476-487
225. Zong H., Ren J.M., Young L.H., Pypaert M., Mu J., Birnbaum M.J., et al. AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. Proc Natl Acad Sci USA 99 (2002) 15983-15987
226. Kiens B. Skeletal muscle lipid metabolism in exercise and insulin resistance. Physiol Rev 86 (2006) 205-243
227. Kruppa J., and Clemens M.J. Differential kinetics of changes in the state of phosphorylation of ribosomal protein S6 and in the rate of protein synthesis in MPC 11 cells during tonicity shifts. EMBO J 3 (1984) 95-100
228. Nygard O., and Nilsson L. Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis. Eur J Biochem 191 (1990) 1-17
229. Giordano E., Cirulli V., Bosco D., Rouiller D., Halban P., and Meda P. -cell size influences glucose-stimulated insulin secretion. Am J Physiol 265 (1993) C358-C364
230. Ono H., Pocai A., Wang Y., Sakoda H., Asano T., Backer J.M., et al. Activation of hypothalamic S6 kinase mediates diet-induced hepatic insulin resistance in rats. J Clin Invest 118 (2008) 2959-2968
231. Antion M.D., Merhav M., Hoeffer C.A., Reis G., Kozma S.C., Thomas G., et al. Removal of S6K1 and S6K2 leads to divergent alterations in learning, memory, and synaptic plasticity. Learn Mem 15 (2008) 29-38