Reactome | MT3 exchanges zinc for copper

MT3 exchanges zinc for copper

Stable Identifier

R-HSA-5662613

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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MT3:7Zn2+ releases 3 zinc ions and binds 4 copper ions at the N-terminal beta domain (Roschitszi et al. 2003, Meloni et al. 2007, Meloni et al. 2008). By this mechanism MT3 is able to scavenge free copper ions and swap metal with an aggregated amyloid beta:copper(II) complex and a alpha-synuclein:copper(II) complex and thereby abolish production of reactive oxygen species (Meloni et al. 2008, Meloni and Vasak 2011, Pedersen et al. 2012, Luo et al. 2013). The copper ions are divalent (copper(II), Cu2+) before binding but univalent (copper(I), Cu1+) after binding (Meloni et al. 2008).

Literature References

PubMed ID	Title	Journal	Year
17389590	Redox silencing of copper in metal-linked neurodegenerative disorders: reaction of Zn7metallothionein-3 with Cu2+ ions Meloni, G, Faller, P, Vasák, M	J. Biol. Chem.	2007
18454142	Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity Meloni, G, Sonois, V, Delaine, T, Guilloreau, L, Gillet, A, Teissié, J, Faller, P, Vasák, M	Nat. Chem. Biol.	2008
21320589	Redox activity of ?-synuclein-Cu is silenced by Zn?-metallothionein-3 Meloni, G, Vašák, M	Free Radic. Biol. Med.	2011
22283439	Rapid exchange of metal between Zn(7)-metallothionein-3 and amyloid-? peptide promotes amyloid-related structural changes Pedersen, JT, Hureau, C, Hemmingsen, L, Heegaard, NH, Østergaard, J, Vašák, M, Faller, P	Biochemistry	2012
23086305	The molecular mechanism for human metallothionein-3 to protect against the neuronal cytotoxicity of A?(1-42) with Cu ions Luo, Y, Xu, Y, Bao, Q, Ding, Z, Zhu, C, Huang, ZX, Tan, X	J. Biol. Inorg. Chem.	2013
12911326	Redox labile site in a Zn4 cluster of Cu4,Zn4-metallothionein-3 Roschitzki, B, Vasák, M	Biochemistry	2003