Acetylation and sumoylation control STAT5 activation antagonistically.

The authors discuss the findings of a study examining the acetylation and sumoylation of STAT5 proteins. They note that sumoylated STAT5 is resulted from impaired STAT5 signaling in lymphocytes isolated from a small ubiquitin-like modifier (SUMO)-specific protease knockout mouse (SENP1-/-). The authors cite the potential of STAT5 to become a target for therapy as acetylation and sumoylation of STAT5 act antagonistically to abolish tyrosine phosphorylation.