English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons15972

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

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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: http://hdl.handle.net/11858/00-001M-0000-0029-2961-C
Abstract
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.