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The MAP kinase phosphorylation site of TAL1 occurs within a transcriptional activation domain.

Alteration of the TAL1 gene is the most common genetic lesion found in patients with T cell acute lymphoblastic leukemia. TAL1 encodes a basic helix-loop-helix transcription factor that is phosphorylated on serine residue 122 by the mitogen-activated protein (MAP) kinase ERK1. Here we show that the amino-terminal sequences of TAL1 (residues 1-166) function in vivo as a transcriptional activation domain. Mutation of serine residue 122 reduces the potency of the transactivation domain by more than half. The data suggest that the amino-terminal transactivation domain of TAL1 is positively regulated by S122 phosphorylation and that the functional properties of TAL1 can be influenced by signal transduction pathways that involve the MAP kinases.