Phosphorylation at Ser²⁶ in the ATP-binding site of Ca²⁺/calmodulin-dependent kinase II as a mechanism for switching off the kinase activity

• Published in: Bioscience reports Vol. 33; no. 2
• Main Authors: Yilmaz, Mehtap, Gangopadhyay, Samudra S, Leavis, Paul, Grabarek, Zenon, Morgan, Kathleen G
• Format: Journal Article
• Language: English
• Published: England Portland Press Ltd 07.02.2013
• Subjects: Adenosine Triphosphate - metabolism; Animals; Binding Sites; Calcium - metabolism; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism; Calmodulin - genetics; Calmodulin - metabolism; Ferrets - genetics; Ferrets - metabolism; Mutation; Original Paper; Phosphorylation - genetics; Protein Isoforms - genetics; Protein Isoforms - metabolism; Serine - genetics; Serine - metabolism; Signal Transduction; Threonine - genetics; Threonine - metabolism

CaMKII (Ca²⁺/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of v...