Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro
作者： D.J. Robbins , E. Zhen , H. Owaki , C.A. Vanderbilt , D. Ebert
DOI: 10.1016/S0021-9258(18)53507-9
关键词:
摘要: Extracellular signal-regulated protein kinases (ERK) 1 and 2 mutants of each were expressed in bacteria with a hexahistidine tag purified using nickel-chelate chromatography. Basal activity wild type ERK2 was approximately nmol/min/mg. Self-catalyzed phosphorylation occurred vitro on the major physiological site tyrosine an intramolecular reaction. Rabbit muscle ERK activator activated 500-1000-fold up to specific (approximately mumol/min/mg) approximating that ERK1 from stimulated cells (Boulton, T.G., Gregory, J.S., Cobb, M.H. (1991) Biochemistry 30, 278-286). could also be by same extent. Mutants lacking autophosphorylated at greatly reduced rate no longer highly kinase. threonine or enhanced rate, but kinase these depended residue used replace threonine. Replacement glutamate rendered capable being activator, while replacement alanine did not. Thus, carboxyl group can provide least some features introduced phosphothreonine ERKs.
elsevier.com
sci-hub.st 参考文章(53)
H. Kosako, Y. Gotoh, S. Matsuda, M. Ishikawa, E. Nishida, Xenopus MAP kinase activator is a serine/threonine/tyrosine kinase activated by threonine phosphorylation. The EMBO Journal. ,vol. 11, pp. 2903- 2908 ,(1992) , 10.1002/J.1460-2075.1992.TB05359.X
S. Matsuda, H. Kosako, K. Takenaka, K. Moriyama, H. Sakai, T. Akiyama, Y. Gotoh, E. Nishida, Xenopus MAP kinase activator: identification and function as a key intermediate in the phosphorylation cascade. The EMBO Journal. ,vol. 11, pp. 973- 982 ,(1992) , 10.1002/J.1460-2075.1992.TB05136.X
S. Nakielny, P. Cohen, J. Wu, T. Sturgill, MAP kinase activator from insulin-stimulated skeletal muscle is a protein threonine/tyrosine kinase The EMBO Journal. ,vol. 11, pp. 2123- 2129 ,(1992) , 10.1002/J.1460-2075.1992.TB05271.X
S. A. Nadin-Davis, A. Nasim, A gene which encodes a predicted protein kinase can restore some functions of the ras gene in fission yeast. The EMBO Journal. ,vol. 7, pp. 985- 993 ,(1988) , 10.1002/J.1460-2075.1988.TB02905.X
D. M. Payne, A. J. Rossomando, P. Martino, A. K. Erickson, J. H. Her, J. Shabanowitz, D. F. Hunt, M. J. Weber, T. W. Sturgill, Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase). The EMBO Journal. ,vol. 10, pp. 885- 892 ,(1991) , 10.1002/J.1460-2075.1991.TB08021.X
J S Gregory, T G Boulton, B C Sang, M H Cobb, An insulin-stimulated ribosomal protein S6 kinase from rabbit liver. Journal of Biological Chemistry. ,vol. 264, pp. 18397- 18401 ,(1989) , 10.1016/S0021-9258(18)51478-2
N G Ahn, E G Krebs, Evidence for an epidermal growth factor-stimulated protein kinase cascade in Swiss 3T3 cells. Activation of serine peptide kinase activity by myelin basic protein kinases in vitro. Journal of Biological Chemistry. ,vol. 265, pp. 11495- 11501 ,(1990) , 10.1016/S0021-9258(19)38424-8
P.D. Adams, P.J. Parker, Activation of mitogen-activated protein (MAP) kinase by a MAP kinase-kinase. Journal of Biological Chemistry. ,vol. 267, pp. 13135- 13137 ,(1992) , 10.1016/S0021-9258(18)42181-3
E. Alvarez, I.C. Northwood, F.A. Gonzalez, D.A. Latour, A. Seth, C. Abate, T. Curran, R.J. Davis, Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase. Journal of Biological Chemistry. ,vol. 266, pp. 15277- 15285 ,(1991) , 10.1016/S0021-9258(18)98613-8
M Hoshi, E Nishida, H Sakai, Activation of a Ca2+-inhibitable protein kinase that phosphorylates microtubule-associated protein 2 in vitro by growth factors, phorbol esters, and serum in quiescent cultured human fibroblasts. Journal of Biological Chemistry. ,vol. 263, pp. 5396- 5401 ,(1988) , 10.1016/S0021-9258(18)60730-6