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

Isobel A. Wadman, Hai Ling Hsu, Melanie H. Cobb, Richard Baer

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

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 languageEnglish (US)
Pages (from-to)3713-3716
Number of pages4
JournalOncogene
Volume9
Issue number12
StatePublished - Dec 1994

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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