Calpain activation

Stable Identifier
Reaction [transition]
Homo sapiens
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Binding of calcium ions to the calpain dimer composed of the calpain catalytic subunit of 80 kDa and a calpain regulatory subunit of 30 kDa enables conformation change that results in formation of a functional catalytic center and also promotes relocalization of the calpain complex to the plasma membrane (Lin et al. 1997, Strobl et al. 2000, Schad et al. 2002). Calpain complexes involving the neuronally expressed mu-calpain (CAPN1) and m-calpain (CAPN2) catalytic subunits (Lee et al. 2000) are shown in this activation reaction.

Literature References
PubMed ID Title Journal Year
10639123 The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium

Strobl, S, Fernandez-Catalan, C, Braun, M, Huber, R, Masumoto, H, Nakagawa, K, Irie, A, Sorimachi, H, Bourenkow, G, Bartunik, H, Suzuki, K, Bode, W

Proc. Natl. Acad. Sci. U.S.A. 2000
11853546 A novel human small subunit of calpains

Schád, E, Farkas, A, Jékely, G, Tompa, P, Friedrich, P

Biochem. J. 2002
10830966 Neurotoxicity induces cleavage of p35 to p25 by calpain

Lee, MS, Kwon, YT, Li, M, Peng, J, Friedlander, RM, Tsai, LH

Nature 2000
9228946 Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding

Lin, GD, Chattopadhyay, D, Mäki, M, Wang, KK, Carson, M, Jin, L, Yuen, PW, Takano, E, Hatanaka, M, DeLucas, LJ, Narayana, SV

Nat. Struct. Biol. 1997
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