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Volumn 269, Issue 22, 2002, Pages 5360-5368

Regulation of peptide-chain elongation in mammalian cells

Author keywords

eEF1; eEF2; Elongation factor; mTOR; Rapamycin; Translation

Indexed keywords

AMINOACYL TRANSFER RNA; CALCIUM ION; CALMODULIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 1BETA; ELONGATION FACTOR 2; INSULIN; PHOSPHATASE;

EID: 0036438894     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03290.x     Document Type: Short Survey
Times cited : (405)

References (75)
  • 1
    • 0036440779 scopus 로고    scopus 로고
    • Regulation of mammalian translation factors by nutrients
    • Proud, C.G. (2002) Regulation of mammalian translation factors by nutrients. Eur. J. Biochem. 269, 5338-5349.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5338-5349
    • Proud, C.G.1
  • 2
    • 0036438924 scopus 로고    scopus 로고
    • Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
    • Scheper, G.C. & Proud, C.G. (2002) Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur. J. Biochem. 269, 5350-5359.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5350-5359
    • Scheper, G.C.1    Proud, C.G.2
  • 3
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translation initiation by FRAP/mTOR
    • Gingras, A.-C., Raught, B. & Sonenberg, N. (2001) Regulation of translation initiation by FRAP/mTOR. Genes Dev. 15, 807-826.
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 4
    • 0035231980 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B
    • Proud, C.G. (2001) Regulation of eukaryotic initiation factor eIF2B. Prog. Mol. Subcell. Biol. 26, 95-114.
    • (2001) Prog. Mol. Subcell. Biol. , vol.26 , pp. 95-114
    • Proud, C.G.1
  • 5
    • 0035371080 scopus 로고    scopus 로고
    • Diversity in translational regulation
    • Macdonald, P. (2001) Diversity in translational regulation. Curr. Opin. Cell. Biol. 13, 326-331.
    • (2001) Curr. Opin. Cell. Biol. , vol.13 , pp. 326-331
    • Macdonald, P.1
  • 6
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever, T.E. (2002) Gene-specific regulation by general translation factors. Cell 108, 545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 7
    • 0002024553 scopus 로고    scopus 로고
    • The protein biosynthesis elongation cycle
    • Sonenberg, N., Hershey, J.W.B. & Mathews, M.B., eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Merrick, W.C. & Nyborg, J. (2000) The protein biosynthesis elongation cycle. In Translational Control of Gene Expression. (Sonenberg, N., Hershey, J.W.B. & Mathews, M.B., eds), pp. 89-125. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 89-125
    • Merrick, W.C.1    Nyborg, J.2
  • 8
    • 0032718056 scopus 로고    scopus 로고
    • Signal transduction pathways that regulate eukaryotic protein synthesis
    • Rhoads, R.E. (1999) Signal transduction pathways that regulate eukaryotic protein synthesis. J. Biol. Chem. 274, 30337-30340.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30337-30340
    • Rhoads, R.E.1
  • 9
    • 0001902617 scopus 로고    scopus 로고
    • Regulation of ribosome recruitment in eukaryotes
    • Sonenberg, N., Hershey, J.W.B. & Mathews, M.B., eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Raught, B., Gingras, A.-C. & Sonenberg, N. (2000) Regulation of ribosome recruitment in eukaryotes. In Translational Control of Gene Expression. (Sonenberg, N., Hershey, J.W.B. & Mathews, M.B., eds), pp. 245-293. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 245-293
    • Raught, B.1    Gingras, A.-C.2    Sonenberg, N.3
  • 10
    • 0035225023 scopus 로고    scopus 로고
    • The p70, S6 kinase integrates nutrient and growth signals to control translational capacity
    • Avruch, J., Belham, C., Weng, Q., Hara, K. & Yonezawa, K. (2001) The p70, S6 kinase integrates nutrient and growth signals to control translational capacity. Prog. Mol. Subcell. Biol. 26, 115-154.
    • (2001) Prog. Mol. Subcell. Biol. , vol.26 , pp. 115-154
    • Avruch, J.1    Belham, C.2    Weng, Q.3    Hara, K.4    Yonezawa, K.5
  • 11
    • 0032788546 scopus 로고    scopus 로고
    • Mutations in elongation factor 1β, a guanine nucleotide exchange factor, enhance translational fidelity
    • Carr-Schmid, A., Valente, L., Loik, V.I., Williams, T., Starita, L.M. & Kinzy, T.G. (1999) Mutations in elongation factor 1β, a guanine nucleotide exchange factor, enhance translational fidelity. Mol. Cell. Biol. 19, 5257-5266.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5257-5266
    • Carr-Schmid, A.1    Valente, L.2    Loik, V.I.3    Williams, T.4    Starita, L.M.5    Kinzy, T.G.6
  • 12
    • 0031467125 scopus 로고    scopus 로고
    • Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli: Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII
    • Sheu, G.T. & Traugh, J.A. (1997) Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli: Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII. J. Biol. Chem. 272, 33290-33297.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33290-33297
    • Sheu, G.T.1    Traugh, J.A.2
  • 13
    • 0035225870 scopus 로고    scopus 로고
    • Insulin, phorbol ester and serum regulate the elongation phase of protein synthesis
    • Traugh, J.A. (2001) Insulin, phorbol ester and serum regulate the elongation phase of protein synthesis. Prog. Mol. Subcell. Biol. 26, 33-48.
    • (2001) Prog. Mol. Subcell. Biol. , vol.26 , pp. 33-48
    • Traugh, J.A.1
  • 14
    • 0033056148 scopus 로고    scopus 로고
    • A structural model for elongation factor (EF-1) and phosphorylation by protein kinase CKII
    • Sheu, G.T. & Traugh, J.A. (1999) A structural model for elongation factor (EF-1) and phosphorylation by protein kinase CKII. Mol. Cell. Biochem. 191, 181-186.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 181-186
    • Sheu, G.T.1    Traugh, J.A.2
  • 15
    • 0035882047 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2B: Identification of multiple phosphorylation sites in the epsilon subunit and their roles in vivo
    • Wang, X., Paulin, F.E.M., Campbell, L.E., Gomez, E., O'Brien, K., Morrice, N. & Proud, C.G. (2001) Eukaryotic initiation factor 2B: Identification of multiple phosphorylation sites in the epsilon subunit and their roles in vivo. EMBO J. 20, 4349-4359.
    • (2001) EMBO J. , vol.20 , pp. 4349-4359
    • Wang, X.1    Paulin, F.E.M.2    Campbell, L.E.3    Gomez, E.4    O'Brien, K.5    Morrice, N.6    Proud, C.G.7
  • 16
    • 0025744934 scopus 로고
    • Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity
    • Venema, R.C., Peters, H.I. & Traugh, J.A. (1991) Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity. J. Biol. Chem. 266, 12574-12580.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12574-12580
    • Venema, R.C.1    Peters, H.I.2    Traugh, J.A.3
  • 17
    • 0026043769 scopus 로고
    • Phosphorylation of valyl-tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities
    • Venema, R.C., Peters, H.I. & Traugh, J.A. (1991) Phosphorylation of valyl-tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities. J. Biol. Chem. 266, 11993-11998.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11993-11998
    • Venema, R.C.1    Peters, H.I.2    Traugh, J.A.3
  • 18
    • 0030725392 scopus 로고    scopus 로고
    • Phosphorylation of elongation factor-1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation
    • Chang, Y.W. & Traugh, J.A. (1997) Phosphorylation of elongation factor-1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation. J. Biol. Chem. 272, 28252-28257.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28252-28257
    • Chang, Y.W.1    Traugh, J.A.2
  • 19
    • 0028892669 scopus 로고
    • Phosphorylation of elongation factor-1 (EF-1) by protein kinase C stimulates GDP/GTP-exchange activity
    • Peters, H.I., Chang, Y.W.E. & Traugh, J.A. (1995) Phosphorylation of elongation factor-1 (EF-1) by protein kinase C stimulates GDP/GTP-exchange activity. Eur. J. Biochem. 234, 550-556.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 550-556
    • Peters, H.I.1    Chang, Y.W.E.2    Traugh, J.A.3
  • 20
    • 0024449630 scopus 로고
    • A purified complex from Xenopus oocytes contains a p47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF-1 gamma and EF-1 beta
    • Belle, R., Derancourt, J., Poulhe, R., Capony, J.P., Ozon, R. & Mulner-Lorillon, O. (1989) A purified complex from Xenopus oocytes contains a p47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF-1 gamma and EF-1 beta. FEBS Lett. 255, 101-104.
    • (1989) FEBS Lett. , vol.255 , pp. 101-104
    • Belle, R.1    Derancourt, J.2    Poulhe, R.3    Capony, J.P.4    Ozon, R.5    Mulner-Lorillon, O.6
  • 21
    • 0025868394 scopus 로고
    • A major substrate of maturation promoting factor identified as elongation factor 1βγδ in Xenopus laevis
    • Janssen, G.M., Morales, J., Schipper, A., Labbe, J.C., Mulner-Lorillon, O., Belle, R. & Moller, W. (1991) A major substrate of maturation promoting factor identified as elongation factor 1βγδ in Xenopus laevis. J. Biol. Chem. 266, 14885-14888.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14885-14888
    • Janssen, G.M.1    Morales, J.2    Schipper, A.3    Labbe, J.C.4    Mulner-Lorillon, O.5    Belle, R.6    Moller, W.7
  • 24
    • 0025868969 scopus 로고
    • Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes
    • Price, N.T., Redpath, N.T., Severinov, K.V., Campbell, D.G., Russell, J.M. & Proud, C.G. (1991) Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes. FEBS Lett. 282, 253-258.
    • (1991) FEBS Lett. , vol.282 , pp. 253-258
    • Price, N.T.1    Redpath, N.T.2    Severinov, K.V.3    Campbell, D.G.4    Russell, J.M.5    Proud, C.G.6
  • 25
    • 0025291205 scopus 로고
    • Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis
    • Nygard, O. & Nilsson, L. (1990) Translational dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis. Eur. J. Biochem. 191, 1-17.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 1-17
    • Nygard, O.1    Nilsson, L.2
  • 26
    • 0024365118 scopus 로고
    • Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocation
    • Ryazanov, A.G. & Davydova, E.K. (1989) Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation. Phosphorylated EF-2 is unable to catalyze translocation. FEBS Lett. 251, 187-190.
    • (1989) FEBS Lett. , vol.251 , pp. 187-190
    • Ryazanov, A.G.1    Davydova, E.K.2
  • 27
    • 0027273725 scopus 로고
    • Regulation of elongation factor-2 by multisite phosphorylation
    • Redpath, N.T., Price, N.T., Severinov, K.V. & Proud, C.G. (1993) Regulation of elongation factor-2 by multisite phosphorylation. Eur. J. Biochem. 213, 689-699.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 689-699
    • Redpath, N.T.1    Price, N.T.2    Severinov, K.V.3    Proud, C.G.4
  • 28
    • 0025003542 scopus 로고
    • Functional properties of phosphorylated elongation factor 2
    • Carlberg, U., Nilsson, A. & Nygard, O. (1990) Functional properties of phosphorylated elongation factor 2. Eur. J. Biochem. 191, 639-645.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 639-645
    • Carlberg, U.1    Nilsson, A.2    Nygard, O.3
  • 29
    • 0024454195 scopus 로고
    • The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2
    • Redpath, N.T. & Proud, C.G. (1989) The tumour promoter okadaic acid inhibits reticulocytelysate protein synthesis by increasing the net phosphorylation of elongation factor 2. Biochem. J. 262, 69-75.
    • (1989) Biochem. J. , vol.262 , pp. 69-75
    • Redpath, N.T.1    Proud, C.G.2
  • 30
    • 0025250558 scopus 로고
    • Activity of protein phosphatases against initiation factor-2 and elongation factor-2
    • Redpath, N.T. & Proud, C.G. (1990) Activity of protein phosphatases against initiation factor-2 and elongation factor-2. Biochem. J. 272, 175-180.
    • (1990) Biochem. J. , vol.272 , pp. 175-180
    • Redpath, N.T.1    Proud, C.G.2
  • 31
    • 0023161505 scopus 로고
    • 2+/calmodulin-dependent phosphorylation of elongation factor 2
    • 2+/calmodulin-dependent phosphorylation of elongation factor 2. FEBS Lett. 214, 331-334.
    • (1987) FEBS Lett. , vol.214 , pp. 331-334
    • Ryazanov, A.G.1
  • 32
    • 0023522187 scopus 로고
    • r 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2
    • r 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. J. Biol. Chem. 262, 17299-17303.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17299-17303
    • Nairn, A.C.1    Palfrey, H.C.2
  • 33
    • 0026566512 scopus 로고
    • 2+-mediated secretion from rat parotid acini
    • 2+-mediated secretion from rat parotid acini. Biochem. J. 282, 877-882.
    • (1992) Biochem. J. , vol.282 , pp. 877-882
    • Hincke, M.T.1    Nairn, A.C.2
  • 34
    • 0024495687 scopus 로고
    • Thrombin and histamine stimulate the phosphorylation of elongation factor 2 in human umbilical vein endothelial cells
    • Mackie, K.P., Nairn, A.C., Hampel, G., Lam, G. & JaKe, E.A. (1989) Thrombin and histamine stimulate the phosphorylation of elongation factor 2 in human umbilical vein endothelial cells. J. Biol. Chem. 264, 1748-1753.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1748-1753
    • Mackie, K.P.1    Nairn, A.C.2    Hampel, G.3    Lam, G.4    Jaffe, E.A.5
  • 35
    • 0025358704 scopus 로고
    • Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesis
    • Celis, J.E., Madsen, P. & Ryazanov, A.G. (1990) Increased phosphorylation of elongation factor 2 during mitosis in transformed human amnion cells correlates with a decreased rate of protein synthesis. Proc. Natl. Acad. Sci. USA 87, 4231-4235.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4231-4235
    • Celis, J.E.1    Madsen, P.2    Ryazanov, A.G.3
  • 36
    • 0027432963 scopus 로고
    • Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas
    • Mitsui, K., Brady, M., Palfrey, H.C. & Nairn, A.C. (1993) Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas. J. Biol. Chem. 268, 13422-13433.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13422-13433
    • Mitsui, K.1    Brady, M.2    Palfrey, H.C.3    Nairn, A.C.4
  • 37
    • 0027510432 scopus 로고
    • Purification and phosphorylation of elongation factor-2 kinase from rabbit reticulocytes
    • Redpath, N.T. & Proud, C.G. (1993) Purification and phosphorylation of elongation factor-2 kinase from rabbit reticulocytes. Eur. J. Biochem. 212, 511-520.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 511-520
    • Redpath, N.T.1    Proud, C.G.2
  • 39
    • 0030016110 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase
    • Redpath, N.T., Price, N.T. & Proud, C.G. (1996) Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase. J. Biol. Chem. 271, 17547-17554.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17547-17554
    • Redpath, N.T.1    Price, N.T.2    Proud, C.G.3
  • 41
    • 0033611493 scopus 로고    scopus 로고
    • Alpha kinases: A new class of protein kinases with a novel catalytic domain
    • Ryazanov, A.G., Pavur, K.S. & Dorovkov, M.V. (1999) Alpha kinases: A new class of protein kinases with a novel catalytic domain. Curr. Biol. 9, R43-R45.
    • (1999) Curr. Biol. , vol.9
    • Ryazanov, A.G.1    Pavur, K.S.2    Dorovkov, M.V.3
  • 42
    • 0037029138 scopus 로고    scopus 로고
    • Elongation factor-2 kinase and its newly discovered relatives
    • Ryazanov, A.G. (2002) Elongation factor-2 kinase and its newly discovered relatives. FEBS Lett. 514, 26-29.
    • (2002) FEBS Lett. , vol.514 , pp. 26-29
    • Ryazanov, A.G.1
  • 43
    • 0032793804 scopus 로고    scopus 로고
    • Analysis of the domain structure of elongation factor-2 kinase by mutagenesis
    • Diggle, T.A., Seehra, C.K., Hase, S. & Redpath, N.T. (1999) Analysis of the domain structure of elongation factor-2 kinase by mutagenesis. FEBS Lett. 457, 189-192.
    • (1999) FEBS Lett. , vol.457 , pp. 189-192
    • Diggle, T.A.1    Seehra, C.K.2    Hase, S.3    Redpath, N.T.4
  • 44
    • 0034633883 scopus 로고    scopus 로고
    • Mapping the functional domains of elongation factor-2 kinase
    • Pavur, K.S., Petrov, A.N. & Ryazanov, A.G. (2000) Mapping the functional domains of elongation factor-2 kinase. Biochemistry 39, 12216-12224.
    • (2000) Biochemistry , vol.39 , pp. 12216-12224
    • Pavur, K.S.1    Petrov, A.N.2    Ryazanov, A.G.3
  • 45
    • 0035947077 scopus 로고    scopus 로고
    • Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity
    • Yamaguchi, H., Matsushita, M., Nairn, A.C. & Kuriyan, J. (2001) Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity. Mol. Cell 7, 1047-1057.
    • (2001) Mol. Cell. , vol.7 , pp. 1047-1057
    • Yamaguchi, H.1    Matsushita, M.2    Nairn, A.C.3    Kuriyan, J.4
  • 46
    • 0030580365 scopus 로고    scopus 로고
    • Elongation factor-2 kinase - Immunological evidence for the existence of tissue-specific isoforms
    • Hait, W.N., Ward, M.D., Trakht, I.N. & Ryazanov, A.G. (1996) Elongation factor-2 kinase - Immunological evidence for the existence of tissue-specific isoforms. FEBS Lett. 397, 55-60.
    • (1996) FEBS Lett. , vol.397 , pp. 55-60
    • Hait, W.N.1    Ward, M.D.2    Trakht, I.N.3    Ryazanov, A.G.4
  • 47
    • 0035793455 scopus 로고    scopus 로고
    • β-Adrenergic agonists increase phosphorylation of elongation factor 2 in car-diomyocytes without eliciting calcium-independent eEF2 kinase activity
    • McLeod, L.E., Wang, L. & Proud, C.G. (2001) β-Adrenergic agonists increase phosphorylation of elongation factor 2 in car-diomyocytes without eliciting calcium-independent eEF2 kinase activity. FEBS Lett. 489, 225-228.
    • (2001) FEBS Lett. , vol.489 , pp. 225-228
    • McLeod, L.E.1    Wang, L.2    Proud, C.G.3
  • 48
    • 0027270901 scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylates rabbit reticulocyte elongation factor-2 kinase and induces calcium-independent activity
    • Redpath, N.T. & Proud, C.G. (1993) Cyclic AMP-dependent protein kinase phosphorylates rabbit reticulocyte elongation factor-2 kinase and induces calcium-independent activity. Biochem. J. 293, 31-34.
    • (1993) Biochem. J. , vol.293 , pp. 31-34
    • Redpath, N.T.1    Proud, C.G.2
  • 50
    • 0032535023 scopus 로고    scopus 로고
    • Regulation of protein synthesis elongation factor-2 kinase by cAMP in adipocytes
    • Diggle, T.A., Redpath, N.T., Heesom, K.J. & Denton, R.M. (1998) Regulation of protein synthesis elongation factor-2 kinase by cAMP in adipocytes. Biochem. J. 336, 525-529.
    • (1998) Biochem. J. , vol.336 , pp. 525-529
    • Diggle, T.A.1    Redpath, N.T.2    Heesom, K.J.3    Denton, R.M.4
  • 52
    • 0029966106 scopus 로고    scopus 로고
    • Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway
    • Redpath, N.T., Foulstone, E.J. & Proud, C.G. (1996) Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway. EMBO J. 15, 2291-2297.
    • (1996) EMBO J. , vol.15 , pp. 2291-2297
    • Redpath, N.T.1    Foulstone, E.J.2    Proud, C.G.3
  • 53
    • 0034107580 scopus 로고    scopus 로고
    • Activation of mRNA translation by insulin in rat cardiomyocytes involves multiple rapamycin-sensitive steps
    • Wang, L., Wang, X. & Proud, C.G. (2000) Activation of mRNA translation by insulin in rat cardiomyocytes involves multiple rapamycin-sensitive steps. Am. J. Physiol. 278, H1056-H1068.
    • (2000) Am. J. Physiol. , vol.278
    • Wang, L.1    Wang, X.2    Proud, C.G.3
  • 55
    • 0034809193 scopus 로고    scopus 로고
    • Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes
    • Everett, A.D., Stoops, T.D., Nairn, A.C. & Brautigan, D. (2001) Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. Am. J. Physiol. 281, H161-H167.
    • (2001) Am. J. Physiol. , vol.281
    • Everett, A.D.1    Stoops, T.D.2    Nairn, A.C.3    Brautigan, D.4
  • 56
    • 0011774969 scopus 로고    scopus 로고
    • Ras/Erk signalling is required for regulation of translation factors linked to mTOR and protein synthesis by hypertrophic agents in cardiomyocytes
    • in press
    • Wang, L. & Proud, C.G. (2002) Ras/Erk signalling is required for regulation of translation factors linked to mTOR and protein synthesis by hypertrophic agents in cardiomyocytes. Circ. Res. in press.
    • (2002) Circ. Res.
    • Wang, L.1    Proud, C.G.2
  • 57
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta
    • Knebel, A., Morrice, N. & Cohen, P. (2001) A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. EMBO J. 20, 4360-4369.
    • (2001) EMBO J. , vol.20 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 58
    • 0036314780 scopus 로고    scopus 로고
    • Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors
    • Patel, J., McLeod, L.E., Vries, R.G., Flynn, A., Wang, X. & Proud, C.G. (2002) Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors. Eur. J. Biochem. 269, 3076-3085.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3076-3085
    • Patel, J.1    McLeod, L.E.2    Vries, R.G.3    Flynn, A.4    Wang, X.5    Proud, C.G.6
  • 59
    • 0037109036 scopus 로고    scopus 로고
    • Stress-induced regulation of eEF2 kinase by SB203580-sensitive and -insensitive pathways
    • Knebel, A., Haydon, C.E., Morrice, N. & Cohen, P. (2002) Stress-induced regulation of eEF2 kinase by SB203580-sensitive and -insensitive pathways. Biochem. J. 367, 525-532.
    • (2002) Biochem. J. , vol.367 , pp. 525-532
    • Knebel, A.1    Haydon, C.E.2    Morrice, N.3    Cohen, P.4
  • 60
    • 0034889904 scopus 로고    scopus 로고
    • Changes in the phosphorylation of initiation factor eIF-2α, elongation factor eEF-2 and p70, S6 kinase after transient focal cerebral ischaemia in mice
    • Althausen, S., Mengesdorf, T., Mies, G., Olah, L., Nairn, A.C., Proud, C.G. & Paschen, W. (2001) Changes in the phosphorylation of initiation factor eIF-2α, elongation factor eEF-2 and p70, S6 kinase after transient focal cerebral ischaemia in mice. J. Neurochem. 78, 779-787.
    • (2001) J. Neurochem. , vol.78 , pp. 779-787
    • Althausen, S.1    Mengesdorf, T.2    Mies, G.3    Olah, L.4    Nairn, A.C.5    Proud, C.G.6    Paschen, W.7
  • 61
    • 0029838333 scopus 로고    scopus 로고
    • Global brain ischemia and reperfusion: Modifications in eukaryotic initiation factors associated with inhibition of translation initiation
    • DeGracia, D.J., Neumar, R.W., White, B.C. & Krause, G.S. (1996) Global brain ischemia and reperfusion: Modifications in eukaryotic initiation factors associated with inhibition of translation initiation. J. Neurochem. 67, 2005-2012.
    • (1996) J. Neurochem. , vol.67 , pp. 2005-2012
    • DeGracia, D.J.1    Neumar, R.W.2    White, B.C.3    Krause, G.S.4
  • 63
    • 0037143449 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis
    • Horman, S., Browne, G.J., Krause, U., Patel, J.V., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C.G. & Rider, M.H. (2002) Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Curr. Biol. 12, 1419-1423.
    • (2002) Curr. Biol. , vol.12 , pp. 1419-1423
    • Horman, S.1    Browne, G.J.2    Krause, U.3    Patel, J.V.4    Vertommen, D.5    Bertrand, L.6    Lavoinne, A.7    Hue, L.8    Proud, C.G.9    Rider, M.H.10
  • 65
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie, D.G., Carling, D. & Carlson, M. (1998) The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67, 821-855.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 66
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the TOR proteins, stimulate the association of Tap42 with Type phosphatases
    • Di Como, C.J. & Arndt, K.T. (1996) Nutrients, via the TOR proteins, stimulate the association of Tap42 with Type phosphatases. Genes Dev. 10, 1904-1916.
    • (1996) Genes Dev. , vol.10 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 68
    • 0033577745 scopus 로고    scopus 로고
    • Tor proteins and protein phosphatase 2A reciprocally regulate Tap42p in controlling cell growth in yeast
    • Jiang, Y. & Broach, J.R. (1999) Tor proteins and protein phosphatase 2A reciprocally regulate Tap42p in controlling cell growth in yeast. EMBO J. 18, 2782-2792.
    • (1999) EMBO J. , vol.18 , pp. 2782-2792
    • Jiang, Y.1    Broach, J.R.2
  • 70
    • 0033543158 scopus 로고    scopus 로고
    • Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favours association with the alpha4 subunit which promotes dephosphorylation of elongation factor-2
    • Chung, H., Nairn, A.C., Murata, K. & Brautigan, D.L. (1999) Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favours association with the alpha4 subunit which promotes dephosphorylation of elongation factor-2. Biochemistry 10, 10371-10376.
    • (1999) Biochemistry , vol.10 , pp. 10371-10376
    • Chung, H.1    Nairn, A.C.2    Murata, K.3    Brautigan, D.L.4
  • 71
    • 0033551234 scopus 로고    scopus 로고
    • Protein phosphatase 2A interacts with the 70 kDa S6 kinase and is activated by inhibition of FKBP-12-rapamycin-associated protein
    • Peterson, R.T., Desai, B.N., Hardwick, J.S. & Schreiber, S.L. (1999) Protein phosphatase 2A interacts with the 70 kDa S6 kinase and is activated by inhibition of FKBP-12-rapamycin-associated protein. Proc. Natl. Acad. Sci. USA 96, 4438-4442.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4438-4442
    • Peterson, R.T.1    Desai, B.N.2    Hardwick, J.S.3    Schreiber, S.L.4
  • 72
    • 0027236459 scopus 로고
    • Phosphorylation of elongation factor-2 from the lepidopteran insect, Spodoptera frugiperda
    • Oldfield, S. & Proud, C.G. (1993) Phosphorylation of elongation factor-2 from the lepidopteran insect, Spodoptera frugiperda. FEBS Lett. 327, 71-74.
    • (1993) FEBS Lett. , vol.327 , pp. 71-74
    • Oldfield, S.1    Proud, C.G.2
  • 73
    • 0034710302 scopus 로고    scopus 로고
    • Protein kinases and phosphatases in the Drosophila genome
    • Morrison, D.K., Murakami, M.S. & Cleghon, V. (2000) Protein kinases and phosphatases in the Drosophila genome. J. Cell. Biol. 150, F57-F62.
    • (2000) J. Cell. Biol. , vol.150
    • Morrison, D.K.1    Murakami, M.S.2    Cleghon, V.3
  • 74
    • 0025997089 scopus 로고
    • Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endogenous kinase
    • Donovan, M.G. & Bodley, J.W. (1991) Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endogenous kinase. FEBS Lett. 291, 303-306.
    • (1991) FEBS Lett. , vol.291 , pp. 303-306
    • Donovan, M.G.1    Bodley, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.