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

Biological Chemistry
G VorbrueggenK Moelling

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.

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Citations

Aug 3, 1999·Journal of Cellular Physiology·E HullemanJ Boonstra
Dec 28, 2010·Clinica Chimica Acta; International Journal of Clinical Chemistry·Mehmet CoskunOle Haagen Nielsen
Jun 15, 2004·Experimental Cell Research·Øyvind DahleOdd Stokke Gabrielsen
May 15, 2007·Oncogene·A G TurjanskiJ S Gutkind
Jan 17, 2003·American Journal of Physiology. Cell Physiology·Hua XuFayez K Ghishan
Mar 1, 2003·The Plant Journal : for Cell and Molecular Biology·Fiona J WoodgerJohn V Jacobsen

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