메뉴 건너뛰기




Volumn 288, Issue 24, 2013, Pages 17803-17811

Proteasomal degradation of eukaryotic elongation factor-2 kinase (EF2K) is regulated by cAMP-PKA signaling and the SCFβTRCP ubiquitin E3 ligase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY-DEPENDENT; ADENOSINE RECEPTOR; CONTROL MECHANISM; DEGRADATION MECHANISM; POLYUBIQUITYLATION; PROTEASOMAL DEGRADATION; PROTEASOME INHIBITORS; PROTEIN TRANSLATION;

EID: 84879064983     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.477182     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 0021523971 scopus 로고
    • Protein synthesis and memory: A review
    • Davis, H. P., and Squire, L. R. (1984) Protein synthesis and memory: a review. Psychol. Bull. 96, 518-559
    • (1984) Psychol. Bull. , vol.96 , pp. 518-559
    • Davis, H.P.1    Squire, L.R.2
  • 3
    • 45149125084 scopus 로고    scopus 로고
    • Protein degradation, as with protein synthesis, is required during not only long-term spatial memory consolidation but also reconsolidation
    • DOI 10.1111/j.1460-9568.2008.06262.x
    • Artinian, J., McGauran, A. M., De Jaeger, X., Mouledous, L., Frances, B., and Roullet, P. (2008) Protein degradation, as with protein synthesis, is required during not only long-term spatial memory consolidation but also reconsolidation. Eur. J. Neurosci. 27, 3009-3019 (Pubitemid 351832218)
    • (2008) European Journal of Neuroscience , vol.27 , Issue.11 , pp. 3009-3019
    • Artinian, J.1    McGauran, A.-M.T.2    De Jaeger, X.3    Mouledous, L.4    Frances, B.5    Roullet, P.6
  • 4
    • 58149469090 scopus 로고    scopus 로고
    • Translational control of long-lasting synaptic plasticity and memory
    • Costa-Mattioli, M., Sossin, W. S., Klann, E., and Sonenberg, N. (2009) Translational control of long-lasting synaptic plasticity and memory. Neuron 61, 10-26
    • (2009) Neuron , vol.61 , pp. 10-26
    • Costa-Mattioli, M.1    Sossin, W.S.2    Klann, E.3    Sonenberg, N.4
  • 5
    • 33646918035 scopus 로고    scopus 로고
    • Involvement of protein synthesis and degradation in long-term potentiation of Schaffer collateral CA1 synapses
    • DOI 10.1523/JNEUROSCI.4573-05.2006
    • Karpova, A., Mikhaylova, M., Thomas, U., Knöpfel, T., and Behnisch, T. (2006) Involvement of protein synthesis and degradation in long-term potentiation of Schaffer collateral CA1 synapses. J. Neurosci. 26, 4949-4955 (Pubitemid 44315337)
    • (2006) Journal of Neuroscience , vol.26 , Issue.18 , pp. 4949-4955
    • Karpova, A.1    Mikhaylova, M.2    Thomas, U.3    Knopfel, T.4    Behnisch, T.5
  • 6
    • 33749620749 scopus 로고    scopus 로고
    • A Balance of Protein Synthesis and Proteasome-Dependent Degradation Determines the Maintenance of LTP
    • DOI 10.1016/j.neuron.2006.08.015, PII S0896627306006374
    • Fonseca, R., Vabulas, R. M., Hartl, F. U., Bonhoeffer, T., and Nägerl, U. V. (2006) A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron 52, 239-245 (Pubitemid 44548341)
    • (2006) Neuron , vol.52 , Issue.2 , pp. 239-245
    • Fonseca, R.1    Vabulas, R.M.2    Hartl, F.U.3    Bonhoeffer, T.4    Nagerl, U.V.5
  • 8
    • 84882882399 scopus 로고    scopus 로고
    • Bradshaw, R. A., and Dennis, E. A., eds, Elsevier, San Francisco
    • Wiseman, S. L., Wei, F. Y., and Nairn, A. C. (2009) in Handbook of Cell Signaling (Bradshaw, R. A., and Dennis, E. A., eds), pp. 587-599, Elsevier, San Francisco
    • (2009) Handbook of Cell Signaling , pp. 587-599
    • Wiseman, S.L.1    Wei, F.Y.2    Nairn, A.C.3
  • 10
    • 34547683444 scopus 로고    scopus 로고
    • Postsynaptic Decoding of Neural Activity: eEF2 as a Biochemical Sensor Coupling Miniature Synaptic Transmission to Local Protein Synthesis
    • DOI 10.1016/j.neuron.2007.07.030, PII S0896627307005752
    • Sutton, M. A., Taylor, A. M., Ito, H. T., Pham, A., and Schuman, E. M. (2007) Postsynaptic decoding of neural activity: eEF2 as a biochemical sensor coupling miniature synaptic transmission to local protein synthesis. Neuron 55, 648-661 (Pubitemid 47223643)
    • (2007) Neuron , vol.55 , Issue.4 , pp. 648-661
    • Sutton, M.A.1    Taylor, A.M.2    Ito, H.T.3    Pham, A.4    Schuman, E.M.5
  • 11
    • 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., and Jaffe, 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 (Pubitemid 19051019)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.3 , pp. 1748-1753
    • Mackie, K.P.1    Nairn, A.C.2    Hampel, G.3    Lam, G.4    Jaffe, E.A.5
  • 12
    • 0023185463 scopus 로고
    • 2+ transients
    • Palfrey, H. C., Nairn, A. C., Muldoon, L. L., and Villereal, M. L. (1987) Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients. J. Biol. Chem. 262, 9785-9792 (Pubitemid 17102621)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.20 , pp. 9785-9792
    • Palfrey, H.C.1    Nairn, A.C.2    Muldoon, L.L.3    Villereal, M.L.4
  • 13
    • 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., and 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 (Pubitemid 23307767)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.18 , pp. 13422-13433
    • Mitsui, K.-I.1    Brady, M.2    Palfrey, H.C.3    Nairn, A.C.4
  • 14
    • 0027270901 scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylates rabbit reticulocyte elongation factor-2 kinase and induces calcium-independent activity
    • Redpath, N. T., and 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 (Pubitemid 23223143)
    • (1993) Biochemical Journal , vol.293 , Issue.1 , pp. 31-34
    • Redpath, N.T.1    Proud, C.G.2
  • 15
    • 0035253165 scopus 로고    scopus 로고
    • 2+/calmodulin-independent activity
    • DOI 10.1042/0264-6021:3530621
    • Diggle, T. A., Subkhankulova, T., Lilley, K. S., Shikotra, N., Willis, A. E., and Redpath, N. T. (2001) Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity. Biochem. J. 353, 621-626 (Pubitemid 32158330)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 621-626
    • Diggle, T.A.1    Subkhankulova, T.2    Lilley, K.S.3    Shikotra, N.4    Willis, A.E.5    Redpath, N.T.6
  • 16
    • 0035881470 scopus 로고    scopus 로고
    • RSK1 and p70 S6 kinase
    • DOI 10.1093/emboj/20.16.4370
    • Wang, X., Li, W., Williams, M., Terada, N., Alessi, D. R., and Proud, C. G. (2001) Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. EMBO J. 20, 4370-4379 (Pubitemid 32772031)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4370-4379
    • Wang, X.1    Li, W.2    Williams, M.3    Terada, N.4    Alessi, D.R.5    Proud, C.G.6
  • 17
    • 1642328617 scopus 로고    scopus 로고
    • Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398
    • DOI 10.1074/jbc.M309773200
    • Browne, G. J., Finn, S. G., and Proud, C. G. (2004) Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. J. Biol. Chem. 279, 12220-12231 (Pubitemid 38445787)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12220-12231
    • Browne, G.J.1    Finn, S.G.2    Proud, C.G.3
  • 19
    • 0025250229 scopus 로고
    • Nerve growth factor-induced down-regulation of calmodulin-dependent protein kinase III in PC12 cells involves cyclic AMP-dependent protein kinase
    • Brady, M. J., Nairn, A. C., Wagner, J. A., and Palfrey, H. C. (1990) Nerve growth factor-induced down-regulation of calmodulin-dependent protein kinase III in PC12 cells involves cyclic AMP-dependent protein kinase. J. Neurochem. 54, 1034-1039
    • (1990) J. Neurochem. , vol.54 , pp. 1034-1039
    • Brady, M.J.1    Nairn, A.C.2    Wagner, J.A.3    Palfrey, H.C.4
  • 20
    • 18144425142 scopus 로고    scopus 로고
    • Identification of the ubiquitin-proteasome pathway in the regulation of the stability of eukaryotic elongation factor-2 kinase
    • DOI 10.1158/0008-5472.CAN-04-4036
    • Arora, S., Yang, J. M., and Hait, W. N. (2005) Identification of the ubiquitin-proteasome pathway in the regulation of the stability of eukaryotic elongation factor-2 kinase. Cancer Res. 65, 3806-3810 (Pubitemid 40616359)
    • (2005) Cancer Research , vol.65 , Issue.9 , pp. 3806-3810
    • Arora, S.1    Yang, J.-M.2    Hait, W.N.3
  • 22
    • 0026681083 scopus 로고
    • Phosphorylation of the cystic fibrosis transmembrane conductance regulator
    • Picciotto, M. R., Cohn, J. A., Bertuzzi, G., Greengard, P., and Nairn, A. C. (1992) Phosphorylation of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 267, 12742-12752
    • (1992) J. Biol. Chem. , vol.267 , pp. 12742-12752
    • Picciotto, M.R.1    Cohn, J.A.2    Bertuzzi, G.3    Greengard, P.4    Nairn, A.C.5
  • 23
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • DOI 10.1038/nrm1471
    • Cardozo, T., and Pagano, M. (2004) The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell. Biol. 5, 739-751 (Pubitemid 39208183)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 24
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • DOI 10.1038/nrm1547
    • Petroski, M. D., and Deshaies, R. J. (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell. Biol. 6, 9-20 (Pubitemid 40064895)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 26
    • 0347361537 scopus 로고    scopus 로고
    • β-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase
    • DOI 10.1101/gad.1157503
    • Jin, J., Shirogane, T., Xu, L., Nalepa, G., Qin, J., Elledge, S. J., and Harper, J. W. (2003) SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase. Genes Dev. 17, 3062-3074 (Pubitemid 38040770)
    • (2003) Genes and Development , vol.17 , Issue.24 , pp. 3062-3074
    • Jin, J.1    Shirogane, T.2    Xu, L.3    Nalepa, G.4    Qin, J.5    Elledge, S.J.6    Harper, J.W.7
  • 27
    • 22844432019 scopus 로고    scopus 로고
    • β-TRCP controls Clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein
    • DOI 10.1074/jbc.M502862200
    • Shirogane, T., Jin, J., Ang, X. L., and Harper, J. W. (2005) SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein. J. Biol. Chem. 280, 26863-26872 (Pubitemid 41040720)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 26863-26872
    • Shirogane, T.1    Jin, J.2    Ang, X.L.3    Harper, J.W.4
  • 28
    • 0033068154 scopus 로고    scopus 로고
    • The SCF(β-TRCP)-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • Winston, J. T., Strack, P., Beer-Romero, P., Chu, C. Y., Elledge, S. J., and Harper, J. W. (1999) The SCFβ-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and beta-catenin and stimulates IκBα ubiquitination in vitro. Genes Dev. 13, 270-283 (Pubitemid 29095799)
    • (1999) Genes and Development , vol.13 , Issue.3 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 29
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers, M. D. (2003) Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 6, 231-242
    • (2003) Nat. Neurosci. , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 31
    • 0034005882 scopus 로고    scopus 로고
    • NMDA receptor-mediated control of protein synthesis at developing synapses
    • DOI 10.1038/72915
    • Scheetz, A. J., Nairn, A. C., and Constantine-Paton, M. (2000) NMDA receptor-mediated control of protein synthesis at developing synapses. Nat. Neurosci. 3, 211-216 (Pubitemid 30140781)
    • (2000) Nature Neuroscience , vol.3 , Issue.3 , pp. 211-216
    • Scheetz, A.J.1    Nairn, A.C.2    Constantine-Paton, M.3
  • 32
    • 33750325725 scopus 로고    scopus 로고
    • S6k1- and βTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth
    • DOI 10.1126/science.1130276
    • Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., and Pagano, M. (2006) S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth. Science 314, 467-471 (Pubitemid 44628968)
    • (2006) Science , vol.314 , Issue.5798 , pp. 467-471
    • Dorrello, N.V.1    Peschiaroli, A.2    Guardavaccaro, D.3    Colburn, N.H.4    Sherman, N.E.5    Pagano, M.6
  • 33
    • 81855228182 scopus 로고    scopus 로고
    • mTOR generates an auto-amplification loop by triggering the βTrCP- and CK1α-dependent degradation of DEPTOR
    • Duan, S., Skaar, J. R., Kuchay, S., Toschi, A., Kanarek, N., Ben-Neriah, Y., and Pagano, M. (2011) mTOR generates an auto-amplification loop by triggering the βTrCP- and CK1α-dependent degradation of DEPTOR. Mol. Cell 44, 317-324
    • (2011) Mol. Cell , vol.44 , pp. 317-324
    • Duan, S.1    Skaar, J.R.2    Kuchay, S.3    Toschi, A.4    Kanarek, N.5    Ben-Neriah, Y.6    Pagano, M.7
  • 35
    • 81855167585 scopus 로고    scopus 로고
    • DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(βTrCP) E3 ubiquitin ligase and regulates survival and autophagy
    • Zhao, Y., Xiong, X., and Sun, Y. (2011) DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(βTrCP) E3 ubiquitin ligase and regulates survival and autophagy. Mol. Cell 44, 304-316
    • (2011) Mol. Cell , vol.44 , pp. 304-316
    • Zhao, Y.1    Xiong, X.2    Sun, Y.3
  • 37
    • 30344449514 scopus 로고    scopus 로고
    • Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila
    • DOI 10.1016/j.cell.2005.12.017, PII S0092867405014042
    • Ashraf, S. I., McLoon, A. L., Sclarsic, S. M., and Kunes, S. (2006) Synaptic protein synthesis associated with memory is regulated by the RISC pathway in Drosophila. Cell 124, 191-205 (Pubitemid 43069319)
    • (2006) Cell , vol.124 , Issue.1 , pp. 191-205
    • Ashraf, S.I.1    McLoon, A.L.2    Sclarsic, S.M.3    Kunes, S.4
  • 38
    • 72149086111 scopus 로고    scopus 로고
    • A coordinated local translational control point at the synapse involving relief from silencing and MOV10 degradation
    • Banerjee, S., Neveu, P., and Kosik, K. S. (2009) A coordinated local translational control point at the synapse involving relief from silencing and MOV10 degradation. Neuron 64, 871-884
    • (2009) Neuron , vol.64 , pp. 871-884
    • Banerjee, S.1    Neveu, P.2    Kosik, K.S.3
  • 39
    • 33746866693 scopus 로고    scopus 로고
    • Dynamic Translational and Proteasomal Regulation of Fragile X Mental Retardation Protein Controls mGluR-Dependent Long-Term Depression
    • DOI 10.1016/j.neuron.2006.07.005, PII S0896627306005459
    • Hou, L., Antion, M. D., Hu, D., Spencer, C. M., Paylor, R., and Klann, E. (2006) Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression. Neuron 51, 441-454 (Pubitemid 44189802)
    • (2006) Neuron , vol.51 , Issue.4 , pp. 441-454
    • Hou, L.1    Antion, M.D.2    Hu, D.3    Spencer, C.M.4    Paylor, R.5    Klann, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.