Acetylation and sumoylation control STAT5 activation antagonistically.
STAT5 proteins are activated by tyrosine phosphorylation, but recently further post-translation modifications such as serine/threonine phosphorylation, acetylation at lysine residues or sumoylation in close vicinity of the critical tyrosine residue have been reported. Here, we discuss new findings on impaired STAT5 signaling in lymphocytes isolated from a SUMO-specific protease knockout mouse (SENP1(-/-)), which results in sumoylated STAT5 and abolishes tyrosine phosphorylation. Van Nguyen and colleagues examined acetylation and sumoylation of STAT5 and found that both modifications act antagonistically to control tyrosine phosphorylation of STAT5.
Center for Molecular Biomedicine; Institute for Biochemistry and Biophysics; Department of Biochemistry; Friedrich Schiller University of Jena; Jena, Germany.
Oliver H
OH
Krämer
Richard
R
Moriggl
STAT5A; STAT5B; acetylation; crosstalk; sumoylation; tyrosine phosphorylation