How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins

Tracey A Rouault; Nunziata Maio

doi:10.1016/j.molcel.2020.03.020

How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins

Mol Cell. 2020 Apr 2;78(1):1-3. doi: 10.1016/j.molcel.2020.03.020.

Authors

Tracey A Rouault¹, Nunziata Maio²

Affiliations

¹ Metals Biology and Molecular Medicine Group, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD, USA. Electronic address: rouault@mail.nih.gov.
² Metals Biology and Molecular Medicine Group, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD, USA.

Abstract

In this issue of Molecular Cell, Wang et al. (2020) discover that the C-terminal substrate-binding domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes FBXL5 binding to IRP2 to effect its oxygen-dependent degradation, unveiling a novel and previously unrecognized mechanism involved in regulation of cellular iron homeostasis.

Published by Elsevier Inc.

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MeSH terms

F-Box Proteins
Homeostasis
Iron*
Oxidation-Reduction
Oxygen*
Sulfur
Ubiquitin-Protein Ligase Complexes

Substances

F-Box Proteins
Sulfur
Iron
Ubiquitin-Protein Ligase Complexes
Oxygen

Grants and funding

Z99 HD999999/ImNIH/Intramural NIH HHS/United States