User menu

Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase.

Bibliographic reference Pyr Dit Ruys, Sébastien ; Wang, Xuemin ; Smith, Ewan M ; Herinckx, Gaëtan ; Hussain, Nusrat ; et. al. Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase.. In: Biochemical Journal, Vol. 442, no.3, p. 681-92 (2012)
Permanent URL http://hdl.handle.net/2078/121140
  1. Ovchinnikov Lev P., Motuz Lyudmila P., Natapov Pavel G., Averbuch Lidiya J., Wettenhall Richard E.H., Szyszka Ryszard, Kramer Gisela, Hardesty Boyd, Three phosphorylation sites in elongation factor 2, 10.1016/0014-5793(90)81473-2
  2. Price Nigel T., Redpath Nicholas T., Severinov Konstantin V., Campbell David G., Russell J.M., Proud Christopher G., Identification of the phosphorylation sites in elongation factor-2 from rabbit reticulocytes, 10.1016/0014-5793(91)80489-p
  3. CARLBERG Ulf, NILSSON Anders, NYGARD Odd, Functional properties of phosphorylated elongation factor 2, 10.1111/j.1432-1033.1990.tb19169.x
  4. Ryazanov Alexey G., Davydova Elena K., Mechanism of elongation factor 2 (EF-2) inactivation upon phosphorylation Phosphorylated EF-2 is unable to catalyze translocation, 10.1016/0014-5793(89)81452-8
  5. Drennan Diana, Ryazanov Alexey G., Alpha-kinases: analysis of the family and comparison with conventional protein kinases, 10.1016/s0079-6107(03)00060-9
  6. Ryazanov Alexey G., Pavur Karen S., Dorovkov Maxim V., Alpha-kinases: a new class of protein kinases with a novel catalytic domain, 10.1016/s0960-9822(99)80006-2
  7. Nairn A. C., Bhagat B., Palfrey H. C., Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues., 10.1073/pnas.82.23.7939
  8. Ryazanov Alexey G., Ca2+/calmodulin-dependent phosphorylation of elongation factor 2, 10.1016/0014-5793(87)80081-9
  9. Pavur Karen S., Petrov Alexey N., Ryazanov Alexey G., Mapping the Functional Domains of Elongation Factor-2 Kinase†, 10.1021/bi0007270
  10. Diggle Tricia A, Seehra Charnjit K, Hase Saiki, Redpath Nicholas T, Analysis of the domain structure of elongation factor-2 kinase by mutagenesis, 10.1016/s0014-5793(99)01034-0
  11. Mittl Peer R.E., Schneider-Brachert Wulf, Sel1-like repeat proteins in signal transduction, 10.1016/j.cellsig.2006.05.034
  12. Yamaguchi Hiroto, Matsushita Masayuki, Nairn Angus C., Kuriyan John, Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity, 10.1016/s1097-2765(01)00256-8
  13. Ye Q., Crawley S. W., Yang Y., Cote G. P., Jia Z., Crystal Structure of the  -Kinase Domain of Dictyostelium Myosin Heavy Chain Kinase A, 10.1126/scisignal.2000525
  14. Smith Ewan M, Proud Christopher G, cdc2–cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner, 10.1038/emboj.2008.39
  15. Wang X., Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase, 10.1093/emboj/20.16.4370
  16. Knebel A., A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta, 10.1093/emboj/20.16.4360
  17. KNEBEL Axel, HAYDON Claire E., MORRICE Nick, COHEN Philip, Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and −insensitive pathways, 10.1042/bj20020916
  18. Browne Gareth J., Finn Stephen G., Proud Christopher G., 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, 10.1074/jbc.m309773200
  19. REDPATH Nicholas T., PROUD Christopher G., Purification and phosphorylation of elongation factor-2 kinase from rabbit reticulocytes, 10.1111/j.1432-1033.1993.tb17688.x
  20. Clark Kristopher, Middelbeek Jeroen, Morrice Nick A., Figdor Carl G., Lasonder Edwin, van Leeuwen Frank N., Massive Autophosphorylation of the Ser/Thr-Rich Domain Controls Protein Kinase Activity of TRPM6 and TRPM7, 10.1371/journal.pone.0001876
  21. Matsushita Masayuki, Kozak J. Ashot, Shimizu Yoshio, McLachlin Derek T., Yamaguchi Hiroto, Wei Fan-Yan, Tomizawa Kazuhito, Matsui Hideki, Chait Brian T., Cahalan Michael D., Nairn Angus C., Channel Function Is Dissociated from the Intrinsic Kinase Activity and Autophosphorylation of TRPM7/ChaK1, 10.1074/jbc.m413671200
  22. Schmitz Carsten, Dorovkov Maxim V., Zhao Xiaoyun, Davenport Bennett J., Ryazanov Alexey G., Perraud Anne-Laure, The Channel Kinases TRPM6 and TRPM7 Are Functionally Nonredundant, 10.1074/jbc.m509175200
  23. Hermosura M. C., Nayakanti H., Dorovkov M. V., Calderon F. R., Ryazanov A. G., Haymer D. S., Garruto R. M., A TRPM7 variant shows altered sensitivity to magnesium that may contribute to the pathogenesis of two Guamanian neurodegenerative disorders, 10.1073/pnas.0505149102
  24. Medley Quintus G., Gariepy Jean, Cote Graham P., Dictyostelium myosin-II heavy-chain kinase A is activated by autophosphorylation: studies with Dictyostelium myosin-II and synthetic peptides, 10.1021/bi00490a016
  25. Crawley Scott W., Gharaei Mojdeh Samimi, Ye Qilu, Yang Yidai, Raveh Barak, London Nir, Schueler-Furman Ora, Jia Zongchao, Côté Graham P., Autophosphorylation ActivatesDictyosteliumMyosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain, 10.1074/jbc.m110.177014
  26. Deprez Johan, Vertommen Didier, Alessi Dario R., Hue Louis, Rider Mark H., Phosphorylation and Activation of Heart 6-Phosphofructo-2-kinase by Protein Kinase B and Other Protein Kinases of the Insulin Signaling Cascades, 10.1074/jbc.272.28.17269
  27. Horman Sandrine, Morel Nicole, Vertommen Didier, Hussain Nusrat, Neumann Dietbert, Beauloye Christophe, Najjar Nicole El, Forcet Christelle, Viollet Benoit, Walsh Michael P., Hue Louis, Rider Mark H., AMP-activated Protein Kinase Phosphorylates and Desensitizes Smooth Muscle Myosin Light Chain Kinase, 10.1074/jbc.m802053200
  28. Woods Angela, Vertommen Didier, Neumann Dietbert, Türk Roland, Bayliss Jayne, Schlattner Uwe, Wallimann Theo, Carling David, Rider Mark H., Identification of Phosphorylation Sites in AMP-activated Protein Kinase (AMPK) for Upstream AMPK Kinases and Study of Their Roles by Site-directed Mutagenesis, 10.1074/jbc.m303946200
  29. Ulintz Peter J., Yocum Anastasia K., Bodenmiller Bernd, Aebersold Ruedi, Andrews Philip C., Nesvizhskii Alexey I., Comparison of MS2-Only, MSA, and MS2/MS3Methodologies for Phosphopeptide Identification, 10.1021/pr800535h
  30. Fonseca Bruno D., Smith Ewan M., Lee Vivian H.-Y., MacKintosh Carol, Proud Christopher G., PRAS40 Is a Target for Mammalian Target of Rapamycin Complex 1 and Is Required for Signaling Downstream of This Complex, 10.1074/jbc.m704406200
  31. Fonseca Bruno D., Alain Tommy, Finestone Leona K., Huang Brandon P. H., Rolfe Mark, Jiang Tian, Yao Zhong, Hernandez Greco, Bennett Christopher F., Proud Christopher G., Pharmacological and Genetic Evaluation of Proposed Roles of Mitogen-activated Protein Kinase/Extracellular Signal-regulated Kinase Kinase (MEK), Extracellular Signal-regulated Kinase (ERK), and p90RSKin the Control of mTORC1 Protein Signaling by Phorbol Esters, 10.1074/jbc.m111.260794
  32. Hall-Jackson Clare A, Cross Darren AE, Morrice Nick, Smythe Carl, ATR is a caffeine-sensitive, DNA-activated protein kinase with a substrate specificity distinct from DNA-PK, 10.1038/sj.onc.1203077
  33. Browne G. J., Proud C. G., A Novel mTOR-Regulated Phosphorylation Site in Elongation Factor 2 Kinase Modulates the Activity of the Kinase and Its Binding to Calmodulin, 10.1128/mcb.24.7.2986-2997.2004
  34. Bradford Marion M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, 10.1016/0003-2697(76)90527-3
  35. Pigott Craig R., Mikolajek Halina, Moore Claire E., Finn Stephen J., Phippen Curtis W., Werner Jörn M., Proud Christopher G., Insights into the regulation of eukaryotic elongation factor 2 kinase and the interplay between its domains, 10.1042/bj20111536
  36. Crawley Scott W., Côté Graham P., Identification of dimer interactions required for the catalytic activity of the TRPM7 alpha-kinase domain, 10.1042/bj20081405
  37. Abramczyk Olga, Tavares Clint D.J., Devkota Ashwini K., Ryazanov Alexey G., Turk Benjamin E., Riggs Austen F., Ozpolat Bulent, Dalby Kevin N., Purification and characterization of tagless recombinant human elongation factor 2 kinase (eEF-2K) expressed in Escherichia coli, 10.1016/j.pep.2011.05.005
  38. Crawley S, Biochim. Biophys. Acta, 1784, 908 (2008)
  39. Olsen Jesper V., Blagoev Blagoy, Gnad Florian, Macek Boris, Kumar Chanchal, Mortensen Peter, Mann Matthias, Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks, 10.1016/j.cell.2006.09.026
  40. Yeaman S, Biochem. J., 162, 411 (1977)
  41. Rodriguez Jesse, Gupta Nitin, Smith Richard D., Pevzner Pavel A., Does Trypsin Cut Before Proline?, 10.1021/pr0705035
  42. Horman Sandrine, Browne Gareth J., Krause Ulrike, Patel Jigna V., Vertommen Didier, Bertrand Luc, Lavoinne Alain, Hue Louis, Proud Christopher G., Rider Mark H., Activation of AMP-Activated Protein Kinase Leads to the Phosphorylation of Elongation Factor 2 and an Inhibition of Protein Synthesis, 10.1016/s0960-9822(02)01077-1
  43. Redpath N, Biochem. J., 293, 31 (1993)
  44. DIGGLE Tricia A., SUBKHANKULOVA Tatiana, LILLEY Kathryn S., SHIKOTRA Nita, WILLIS Anne E., REDPATH Nicholas T., Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity, 10.1042/0264-6021:3530621
  45. Crawley Scott W., Liburd Janine, Shaw Kristopher, Jung Yoojin, Smith Steven P., Côté Graham P., Identification of Calmodulin and MlcC as Light Chains forDictyosteliumMyosin-I Isozymes, 10.1021/bi2007178
  46. Horman Sandrine, Vertommen Didier, Heath Richard, Neumann Dietbert, Mouton Véronique, Woods Angela, Schlattner Uwe, Wallimann Theo, Carling David, Hue Louis, Rider Mark H., Insulin Antagonizes Ischemia-induced Thr172Phosphorylation of AMP-activated Protein Kinase α-Subunits in Heart via Hierarchical Phosphorylation of Ser485/491, 10.1074/jbc.m506850200