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. 2011 Feb 24;434(Pt 3):365–381. doi: 10.1042/BJ20101825

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© 2011 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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IRP2 is stable in iron deficient and/or hypoxic cells; under these conditions, FBXL5 undergoes ubiquitination and proteasomal degradation. An increase in iron and oxygen levels stabilizes FBXL5 by formation of an Fe–O–Fe centre in its haemerythrin domain, triggering the assembly of an E3 ubiquitin ligase complex together with Skp1, Cul1 and Rbx1. This complex ubiquitinates (Ub) IRP2, leading to its recognition by the proteasome and its degradation.