This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cheng, J T Articles by Baer, R Search for Related Content PubMed PubMed Citation Articles by Cheng, J T Articles by Baer, R

 Previous Article  |  Next Article 

Mol Cell Biol. 1993 February; 13(2): 801-808

Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1.

Department of Microbiology, University of Texas Southwestern Medical Center, Dallas 75235.

ABSTRACT

Alteration of the TAL1 gene is the most common genetic lesion found in T-cell acute lymphoblastic leukemia. TAL1 encodes phosphoproteins, pp42TAL1 and pp22TAL1, that represent phosphorylated versions of the full-length (residues 1 to 331) and truncated (residues 176 to 331) TAL1 gene products, respectively. Both proteins contain the basic helix-loop-helix motif, a DNA-binding and protein dimerization motif common to several known transcriptional regulatory factors. We now report that serine residue 122 (S122) is a major phosphorylation site of pp42TAL1 in leukemic cell lines and transfected COS1 cells. In vivo phosphorylation of S122 is induced by epidermal growth factor with a rapid time course that parallels activation of the ERK/MAP2 protein kinases. Moreover, S122 is readily phosphorylated in vitro by the extracellular signal-regulated protein kinase ERK1. These data suggest that TAL1 residue S122 serves as an in vivo substrate for ERK/MAP2 kinases such as ERK1. Therefore, S122 phosphorylation may provide a mechanism whereby the properties of TAL1 polypeptides can be modulated by extracellular stimuli.

This article has been cited by other articles:

• Tang, T., Arbiser, J. L., Brandt, S. J. (2002). Phosphorylation by Mitogen-activated Protein Kinase Mediates the Hypoxia-induced Turnover of the TAL1/SCL Transcription Factor in Endothelial Cells. J. Biol. Chem. 277: 18365-18372 [Abstract] [Full Text]  
• Wei, S., Gilvary, D. L., Corliss, B. C., Sebti, S., Sun, J., Straus, D. B., Leibson, P. J., Trapani, J. A., Hamilton, A. D., Weber, M. J., Djeu, J. Y. (2000). Direct Tumor Lysis by NK Cells Uses a Ras-Independent Mitogen-Activated Protein Kinase Signal Pathway. J. Immunol. 165: 3811-3819 [Abstract] [Full Text]  
• Bates, M. E., Green, V. L., Bertics, P. J. (2000). ERK1 and ERK2 Activation by Chemotactic Factors in Human Eosinophils Is Interleukin 5-dependent and Contributes to Leukotriene C4 Biosynthesis. J. Biol. Chem. 275: 10968-10975 [Abstract] [Full Text]  
• Courtes, C., Lecointe, N., Le Cam, L., Baudoin, F., Sardet, C., Mathieu-Mahul, D. (2000). Erythroid-specific Inhibition of the tal-1 Intragenic Promoter Is Due to Binding of a Repressor to a Novel Silencer. J. Biol. Chem. 275: 949-958 [Abstract] [Full Text]  
• Shirakata, Y., Ishii, K., Yagita, H., Okumura, K., Taniguchi, M., Takemori, T. (1999). Distinct Subcellular Localization and Substrate Specificity of Extracellular Signal-Regulated Kinase in B Cells upon Stimulation with IgM and CD40. J. Immunol. 163: 6589-6597 [Abstract] [Full Text]  
• Hochholdinger, F., Baier, G., Nogalo, A., Bauer, B., Grunicke, H. H., Uberall, F. (1999). Novel Membrane-Targeted ERK1 and ERK2 Chimeras Which Act as Dominant Negative, Isotype-Specific Mitogen-Activated Protein Kinase Inhibitors of Ras-Raf-Mediated Transcriptional Activation of c-fos in NIH 3T3 Cells. Mol. Cell. Biol. 19: 8052-8065 [Abstract] [Full Text]  
• Begley, C. G., Green, A. R. (1999). The SCL Gene: From Case Report to Critical Hematopoietic Regulator. Blood 93: 2760-2770 [Full Text]  
• Lu, Q., Paredes, M., Zhang, J., Kosik, K. S. (1998). Basal Extracellular Signal-Regulated Kinase Activity Modulates Cell-Cell and Cell-Matrix Interactions. Mol. Cell. Biol. 18: 3257-3265 [Abstract] [Full Text]  
• Hallek, M., Leif Bergsagel, P., Anderson, K. C. (1998). Multiple Myeloma: Increasing Evidence for a Multistep Transformation Process. Blood 91: 3-21 [Full Text]  
• Prasad, K. S.S., Brandt, S. J. (1997). Target-dependent Effect of Phosphorylation on the DNA Binding Activity of the TAL1/SCL Oncoprotein. J. Biol. Chem. 272: 11457-11462 [Abstract] [Full Text]  
• Whitehurst, C. E., Owaki, H., Bruder, J. T., Rapp, U. R., Geppert, T. D. (1995). The MEK Kinase Activity of the Catalytic Domain of RAF-1 Is Regulated Independently of Ras Binding in T Cells. J. Biol. Chem. 270: 5594-5599 [Abstract] [Full Text]  
• Habelhah, H., Shah, K., Huang, L., Burlingame, A. L., Shokat, K. M., Ronai, Z.'e. (2001). Identification of New JNK Substrate Using ATP Pocket Mutant JNK and a Corresponding ATP Analogue. J. Biol. Chem. 276: 18090-18095 [Abstract] [Full Text]  
• Buschmann, T., Yin, Z., Bhoumik, A., Ronai, Z.'e. (2000). Amino-terminal-derived JNK Fragment Alters Expression and Activity of c-Jun, ATF2, and p53 and Increases H2O2-induced Cell Death. J. Biol. Chem. 275: 16590-16596 [Abstract] [Full Text]