NDLI: Evidence that phosphorylation of iron regulatory protein 1 at Serine 138 destabilizes the [4Fe-4S] cluster in cytosolic aconitase by enhancing 4Fe-3Fe cycling.

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Evidence that phosphorylation of iron regulatory protein 1 at Serine 138 destabilizes the [4Fe-4S] cluster in cytosolic aconitase by enhancing 4Fe-3Fe cycling.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Anderson, Sheila A. Vasanthakumar, Aparna Eisenstein, Richard S. Goforth, Jeremy B. Deck, Kathryn M. Antholine, William E. Kennedy, M. Claire
Description	Author Affiliation: Deck KM ( Department of Nutritional Sciences, University of Wisconsin-Madison, Madison, WI 53706, USA.)
Abstract	Iron-sulfur cluster-dependent interconversion of iron regulatory protein 1 (IRP1) between its RNA binding and cytosolic aconitase (c-acon) forms controls vertebrate iron homeostasis. Cluster removal from c-acon is thought to include oxidative demetallation as a required step, but little else is understood about the process of conversion to IRP1. In comparison with c-acon(WT), Ser(138) phosphomimetic mutants of c-acon contain an unstable [4Fe-4S] cluster and were used as tools to further define the pathway(s) of iron-sulfur cluster disassembly. Under anaerobic conditions cluster insertion into purified IRP1(S138E) and cluster loss on treatment with NO regulated aconitase and RNA binding activity over a similar range as observed for IRP1(WT). However, activation of RNA binding of c-acon(S138E) was an order of magnitude more sensitive to NO than for c-acon(WT). Consistent with this, an altered set point between RNA-binding and aconitase forms was observed for IRP1(S138E) when expressed in HEK cells. Active c-acon(S138E) could only accumulate under hypoxic conditions, suggesting enhanced cluster disassembly in normoxia. Cluster disassembly mechanisms were further probed by determining the impact of iron chelation on acon activity. Unexpectedly EDTA rapidly inhibited c-acon(S138E) activity without affecting c-acon(WT). Additional chelator experiments suggested that cluster loss can be initiated in c-acon(S138E) through a spontaneous nonoxidative demetallation process. Taken together, our results support a model wherein Ser(138) phosphorylation sensitizes IRP1/c-acon to decreased iron availability by allowing the [4Fe-4S](2+) cluster to cycle with [3Fe-4S](0) in the absence of cluster perturbants, indicating that regulation can be initiated merely by changes in iron availability.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	19
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-05-08
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aconitate Hydratase Metabolism Iron Regulatory Protein 1 Iron-Sulfur Proteins Serine Cytosol Enzymology Electron Spin Resonance Spectroscopy Anoxia Iron Chelating Agents Genetics Kidney Cytology Mutagenesis, Site-Directed Mutation Nitric Oxide Phosphorylation RNA Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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