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- W1966392807 abstract "Zn2+ is an essential micronutrient for the growth and development of multicellular organisms, as Zn2+ deficiencies lead to growth retardation and congenital malformations (Vallee, BL, Falchuk, KH. 1993. Physiol Rev., 73:79–118). At the cellular level Zn2+ depravation results in proliferation defects in many cell types (Vallee, BL, Falchuk, KH. 1993. Physiol Rev., 73:79–118), however the molecular pathways involved remain poorly defined. Here we show that the transition metal chelator TPEN (N,N,N′,N′-tetrakis(2-pyridylmethyl) ethylene diamine) blocks the G2/M transition of the meiotic cell cycle by inhibiting Cdc25C-cdk1 activation. ICP-MS analyses reveal that Cdc25C is a Zn2+-binding metalloprotein, and that TPEN effectively strips Zn2+ away from the enzyme. Interestingly, although apo-Cdc25C (Zn2+-deficient) remains fully catalytically active, it is compromised in its ability to dephosphorylate and activate MPF/cdk1. Thus, Zn2+ is an important regulator of Cdc25C function in vivo. Because of the conserved essential role of the Cdc25C-cdk1 module in the eukaryotic cell cycle, these studies provide fundamental insights into cell cycle regulation. J. Cell. Physiol. 213: 98–104, 2007. © 2007 Wiley-Liss, Inc." @default.
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- W1966392807 date "2007-01-01" @default.
- W1966392807 modified "2023-10-03" @default.
- W1966392807 title "Zinc regulates the ability of Cdc25C to activate MPF/cdk1" @default.
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- W1966392807 doi "https://doi.org/10.1002/jcp.21090" @default.
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