Activation of Calcineurin

Stable Identifier
Reaction [binding]
Homo sapiens
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Calcineurin (CaN), also called protein phosphatase 2B (PP2B), is a calcium/Calmodulin (CaM)-dependent serine/threonine protein phosphatase. It exists as a heterodimer consisting of CaM-binding catalytic subunit CaN A chain and a Ca+2 binding regulatory CaN B chain. At low calcium concentrations, CaN exists in an inactive state, where the autoinhibitory domain (AID) binds to the active-site cleft. Upon an increase in calcium concentration CaM binds to Ca+2 ions and gets activated. Active CaM binds to CaN regulatory domain (RD) and this causes release of the AID and activation of the phosphatase (Rumi-Masante et al. 2012). Binding of calcium to CaN B regulatory chain also causes a conformational change of the RD of CaN A chain (Yang & Klee 2000).

Literature References
PubMed ID Title Journal Year
18296442 The secondary structure of calcineurin regulatory region and conformational change induced by calcium/calmodulin binding

Shen, X, Li, H, Ou, Y, Tao, W, Dong, A, Kong, J, Ji, C, Yu, S

J. Biol. Chem. 2008
11015619 Calcineurin: form and function

Rusnak, F, Mertz, P

Physiol. Rev. 2000
Participant Of
Orthologous Events