Abstract
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.
Original language | English (US) |
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Pages (from-to) | 3713-3716 |
Number of pages | 4 |
Journal | Oncogene |
Volume | 9 |
Issue number | 12 |
State | Published - Dec 1994 |
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Cancer Research