메뉴 건너뛰기




Volumn 136, Issue 2, 2016, Pages 276-284

Eukaryotic elongation factor 2 kinase regulates the synthesis of microtubule-related proteins in neurons

Author keywords

elongation; mass spectrometry; microtubules; primary neurons; SILAC; translational control

Indexed keywords

ELONGATION FACTOR 2 KINASE; MESSENGER RNA; AMINO ACID; ENZYME INHIBITOR; ISOTOPE; MICROTUBULE PROTEIN; N ETHYLMALEIMIDE SENSITIVE FACTOR; NSF PROTEIN, MOUSE;

EID: 84954394192     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13407     Document Type: Article
Times cited : (40)

References (32)
  • 1
    • 28744451770 scopus 로고    scopus 로고
    • A molecular switch for translational control in taste memory consolidation
    • Belelovsky K., Elkobi A., Kaphzan H., Nairn A. C., and, Rosenblum K., (2005) A molecular switch for translational control in taste memory consolidation. Eur. J. Neurosci. 22, 2560-2568.
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 2560-2568
    • Belelovsky, K.1    Elkobi, A.2    Kaphzan, H.3    Nairn, A.C.4    Rosenblum, K.5
  • 2
    • 36849034953 scopus 로고    scopus 로고
    • Characterization of the role of microtubule-associated protein 1B in metabotropic glutamate receptor-mediated endocytosis of AMPA receptors in hippocampus
    • Davidkova G., and, Carroll R. C., (2007) Characterization of the role of microtubule-associated protein 1B in metabotropic glutamate receptor-mediated endocytosis of AMPA receptors in hippocampus. J. Neurosci. 27, 13273-13278.
    • (2007) J. Neurosci. , vol.27 , pp. 13273-13278
    • Davidkova, G.1    Carroll, R.C.2
  • 3
    • 33745464039 scopus 로고    scopus 로고
    • Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT)
    • Dieterich D. C., Link A. J., Graumann J., Tirrell D. A., and, Schuman E. M., (2006) Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT). Proc. Natl Acad. Sci. USA 103, 9482-9487.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9482-9487
    • Dieterich, D.C.1    Link, A.J.2    Graumann, J.3    Tirrell, D.A.4    Schuman, E.M.5
  • 4
    • 77952889767 scopus 로고    scopus 로고
    • Changes in microtubule turnover accompany synaptic plasticity and memory formation in response to contextual fear conditioning in mice
    • Fanara P., Husted K. H., Selle K., Wong P. Y., Banerjee J., Brandt R., and, Hellerstein M. K., (2010) Changes in microtubule turnover accompany synaptic plasticity and memory formation in response to contextual fear conditioning in mice. Neuroscience 168, 167-178.
    • (2010) Neuroscience , vol.168 , pp. 167-178
    • Fanara, P.1    Husted, K.H.2    Selle, K.3    Wong, P.Y.4    Banerjee, J.5    Brandt, R.6    Hellerstein, M.K.7
  • 5
    • 84921503014 scopus 로고    scopus 로고
    • BDNF stimulation of protein synthesis in cortical neurons requires the MAP kinase-interacting kinase MNK1
    • Genheden M., Kenney J. W., Johnston H. E., Manousopoulou A., Garbis S. D., and, Proud C. G., (2015) BDNF stimulation of protein synthesis in cortical neurons requires the MAP kinase-interacting kinase MNK1. J. Neurosci. 35, 972-984.
    • (2015) J. Neurosci. , vol.35 , pp. 972-984
    • Genheden, M.1    Kenney, J.W.2    Johnston, H.E.3    Manousopoulou, A.4    Garbis, S.D.5    Proud, C.G.6
  • 7
    • 84862281980 scopus 로고    scopus 로고
    • Cycloheximide impairs and enhances memory depending on dose and footshock intensity
    • Gold P. E., and, Wrenn S. M., (2012) Cycloheximide impairs and enhances memory depending on dose and footshock intensity. Behav. Brain Res. 233, 293-297.
    • (2012) Behav. Brain Res. , vol.233 , pp. 293-297
    • Gold, P.E.1    Wrenn, S.M.2
  • 8
    • 58149225472 scopus 로고    scopus 로고
    • Microtubules in dendritic spine development
    • Gu J., Firestein B. L., and, Zheng J. Q., (2008) Microtubules in dendritic spine development. J. Neurosci. 28, 12120-12124.
    • (2008) J. Neurosci. , vol.28 , pp. 12120-12124
    • Gu, J.1    Firestein, B.L.2    Zheng, J.Q.3
  • 10
    • 84875755186 scopus 로고    scopus 로고
    • QuaNCAT: Quantitating proteome dynamics in primary cells
    • Howden A. J., Geoghegan V., Katsch K., et al,. (2013) QuaNCAT: quantitating proteome dynamics in primary cells. Nat. Methods 10, 343-346.
    • (2013) Nat. Methods , vol.10 , pp. 343-346
    • Howden, A.J.1    Geoghegan, V.2    Katsch, K.3
  • 11
    • 58149272090 scopus 로고    scopus 로고
    • Activity-dependent dynamic microtubule invasion of dendritic spines
    • Hu X., Viesselmann C., Nam S., Merriam E., and, Dent E. W., (2008) Activity-dependent dynamic microtubule invasion of dendritic spines. J. Neurosci. 28, 13094-13105.
    • (2008) J. Neurosci. , vol.28 , pp. 13094-13105
    • Hu, X.1    Viesselmann, C.2    Nam, S.3    Merriam, E.4    Dent, E.W.5
  • 12
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang dW, Sherman BT, and, Lempicki RA, (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57.
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.1    Sherman, B.T.2    Lempicki, R.A.3
  • 13
    • 84860805752 scopus 로고    scopus 로고
    • Stable isotope-labelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis
    • Huo Y., Iadevaia V., Yao Z., Kelly I., Cosulich S., Guichard S., Foster L. J., and, Proud C. G., (2012) Stable isotope-labelling analysis of the impact of inhibition of the mammalian target of rapamycin on protein synthesis. Biochem. J. 444, 141-151.
    • (2012) Biochem. J. , vol.444 , pp. 141-151
    • Huo, Y.1    Iadevaia, V.2    Yao, Z.3    Kelly, I.4    Cosulich, S.5    Guichard, S.6    Foster, L.J.7    Proud, C.G.8
  • 14
    • 77949324458 scopus 로고    scopus 로고
    • Post-training dephosphorylation of eEF-2 promotes protein synthesis for memory consolidation
    • Im H. I., Nakajima A., Gong B., Xiong X., Mamiya T., Gershon E. S., Zhuo M., and, Tang Y. P., (2009) Post-training dephosphorylation of eEF-2 promotes protein synthesis for memory consolidation. PLoS ONE 4, e7424.
    • (2009) PLoS ONE , vol.4 , pp. e7424
    • Im, H.I.1    Nakajima, A.2    Gong, B.3    Xiong, X.4    Mamiya, T.5    Gershon, E.S.6    Zhuo, M.7    Tang, Y.P.8
  • 15
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • Ingolia N. T., Lareau L. F., and, Weissman J. S., (2011) Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147, 789-802.
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 16
    • 58149214025 scopus 로고    scopus 로고
    • Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity
    • Jaworski J., Kapitein L. C., Gouveia S. M., et al,. (2009) Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity. Neuron 61, 85-100.
    • (2009) Neuron , vol.61 , pp. 85-100
    • Jaworski, J.1    Kapitein, L.C.2    Gouveia, S.M.3
  • 17
    • 84901463783 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles
    • Kenney J. W., Moore C. E., Wang X., and, Proud C. G., (2014) Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles. Adv. Biol. Regul. 55C, 15-27.
    • (2014) Adv. Biol. Regul. , vol.55 C , pp. 15-27
    • Kenney, J.W.1    Moore, C.E.2    Wang, X.3    Proud, C.G.4
  • 19
    • 46149087988 scopus 로고    scopus 로고
    • Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/Arg3.1 essential for mGluR-LTD
    • Park S., Park J. M., Kim S., et al,. (2008) Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/Arg3.1 essential for mGluR-LTD. Neuron 59, 70-83.
    • (2008) Neuron , vol.59 , pp. 70-83
    • Park, S.1    Park, J.M.2    Kim, S.3
  • 20
    • 0027273725 scopus 로고
    • Regulation of elongation factor-2 by multisite phosphorylation
    • Redpath N. T., Price N. T., Severinov K. V., and, 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
  • 21
    • 0023884601 scopus 로고
    • Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation
    • Ryazanov A. G., Shestakova E. A., and, Natapov P. G., (1988) Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation. Nature 334, 170-173.
    • (1988) Nature , vol.334 , pp. 170-173
    • Ryazanov, A.G.1    Shestakova, E.A.2    Natapov, P.G.3
  • 22
    • 0034005882 scopus 로고    scopus 로고
    • NMDA receptor-mediated control of protein synthesis at developing synapses
    • 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.
    • (2000) Nat. Neurosci. , vol.3 , pp. 211-216
    • Scheetz, A.J.1    Nairn, A.C.2    Constantine-Paton, M.3
  • 23
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • Schwanhausser B., Gossen M., Dittmar G., and, Selbach M., (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9, 205-209.
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhausser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 24
    • 84910010088 scopus 로고    scopus 로고
    • Nervous translation, do you get the message? A review of mRNPs, mRNA-protein interactions and translational control within cells of the nervous system
    • Smith R., Rathod R. J., Rajkumar S., and, Kennedy D., (2014) Nervous translation, do you get the message? A review of mRNPs, mRNA-protein interactions and translational control within cells of the nervous system. Cell. Mol. Life Sci. 71, 3917-3937.
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 3917-3937
    • Smith, R.1    Rathod, R.J.2    Rajkumar, S.3    Kennedy, D.4
  • 25
    • 84870393190 scopus 로고    scopus 로고
    • Identification and quantification of newly synthesized proteins translationally regulated by YB-1 using a novel Click-SILAC approach
    • Somasekharan S. P., Stoynov N., Rotblat B., Leprivier G., Galpin J. D., Ahern C. A., Foster L. J., and, Sorensen P. H., (2012) Identification and quantification of newly synthesized proteins translationally regulated by YB-1 using a novel Click-SILAC approach. J. Proteomics. 77, e1-e10.
    • (2012) J. Proteomics. , vol.77 , pp. e1-e10
    • Somasekharan, S.P.1    Stoynov, N.2    Rotblat, B.3    Leprivier, G.4    Galpin, J.D.5    Ahern, C.A.6    Foster, L.J.7    Sorensen, P.H.8
  • 29
    • 85018035208 scopus 로고    scopus 로고
    • Abstract 3229: Managing stress: Discovery of inhibitors of the atypical kinase eEF2K and the class III PI3K, VPS34
    • Versele M., Moore C., Proud C. G., et al,. (2014) Abstract 3229: Managing stress: discovery of inhibitors of the atypical kinase eEF2K and the class III PI3K, VPS34. Cancer Res. 74, 3229.
    • (2014) Cancer Res. , vol.74 , pp. 3229
    • Versele, M.1    Moore, C.2    Proud, C.G.3
  • 30
    • 0022450047 scopus 로고
    • Translational control of gene expression in a normal fibroblast. Characterization of a subclass of mRNAs with unusual kinetic properties
    • Walden W. E., and, Thach R. E., (1986) Translational control of gene expression in a normal fibroblast. Characterization of a subclass of mRNAs with unusual kinetic properties. Biochemistry 25, 2033-2041.
    • (1986) Biochemistry , vol.25 , pp. 2033-2041
    • Walden, W.E.1    Thach, R.E.2
  • 31
    • 0019888554 scopus 로고
    • The role of mRNA competition in regulating translation. I. Demonstration of competition in vivo
    • Walden W. E., Godefroy-Colburn T., and, Thach R. E., (1981) The role of mRNA competition in regulating translation. I. Demonstration of competition in vivo. J. Biol. Chem. 256, 11739-11746.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11739-11746
    • Walden, W.E.1    Godefroy-Colburn, T.2    Thach, R.E.3
  • 32
    • 25444483560 scopus 로고    scopus 로고
    • Mutually exclusive subsets of BH3-only proteins are activated by the p53 and c-Jun N-terminal kinase/c-Jun signaling pathways during cortical neuron apoptosis induced by arsenite
    • Wong H. K., Fricker M., Wyttenbach A., Villunger A., Michalak E. M., Strasser A., and, Tolkovsky A. M., (2005) Mutually exclusive subsets of BH3-only proteins are activated by the p53 and c-Jun N-terminal kinase/c-Jun signaling pathways during cortical neuron apoptosis induced by arsenite. Mol. Cell. Biol. 25, 8732-8747.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8732-8747
    • Wong, H.K.1    Fricker, M.2    Wyttenbach, A.3    Villunger, A.4    Michalak, E.M.5    Strasser, A.6    Tolkovsky, A.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.