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Atypon Free PMC Article

Mol Cell Biol. 1993 Feb;13(2):801-8. doi: 10.1128/mcb.13.2.801-808.1993.

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

Molecular and cellular biology

J T Cheng, M H Cobb, R Baer

Affiliations

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

PMID: 8423803 PMCID: PMC358963 DOI: 10.1128/mcb.13.2.801-808.1993
Free PMC Article

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.

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