Functional analysis of phosphorylation at serine 532 of human c-Myb by MAP kinase

Gerd Vorbrueggen, Josip Lovrić, Karin Moelling

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    The c-myb proto-oncogene encodes a transcription factor that is implicated in regulatory events during hematopoiesis. It contains negative regulatory domains at both the amino- and carboxy-termini. Here we describe that human c-Myb can be phosphorylated by mitogen-activated protein kinases (MAPK's) at serine 532 of the carboxy (C-) terminal regulatory domain in vitro. This serine residue can also be phosphorylated in vivo upon serum-stimulation of Jurkat cells. Expression of a constitutively active form of Ras together with c-Myb in transient transfection experiments had no effect on the transcriptional activity of c-Myb, while expression of a polypeptide containing the c-Myb C-terminal domain stimulated c-Myb activity. This effect is reduced upon MAPK-dependent phosphorylation of serine 532. Our data suggest that the MAPK-dependent state of phosphorylation modifies the cellular function of c-Myb by modulating its interaction with a putative inhibitory factor.
    Original languageEnglish
    Pages (from-to)721-730
    Number of pages9
    JournalBiological Chemistry
    Issue number11
    Publication statusPublished - Nov 1996


    • c-Myb inhibitor
    • c-Myb regulation
    • Mitogen activated protein kinases
    • Phosphopeptide mapping
    • Serum stimulation
    • Transcriptional activation


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