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Journal Article

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


Vorbrüggen,  G.
Research Group of Molecular Cell Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Vorbrüggen, G., Lovric, J., & Mölling, K. (1996). Functional analysis of phosphorylation at serine 532 of human c-Myb by MAP kinase. Biological Chemistry, 377(11), 721-730.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-2961-C
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.