[HTML][HTML] Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification

WB Dias, WD Cheung, Z Wang, GW Hart - Journal of Biological Chemistry, 2009 - ASBMB
Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser (Thr) residues on
polypeptides) is an abundant, dynamic, and inducible post-translational modification.
GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including
signaling, cell cycle, and transcription. Here we show that calcium/calmodulin-dependent
kinase IV (CaMKIV) is highly GlcNAcylated in vivo. In addition, we show that upon activation
of HEK293 cells, hemagglutinin-tagged CaMKIV GlcNAcylation rapidly decreases, in a …