The iron-responsive element binding protein: a target for synaptic actions of nitric oxide

Molecular targets for the actions of nitric oxide (NO) have only been partially clarified. The dynamic properties of the iron-sulfur (Fe-S) cluster of the iron responsive-element binding protein (IRE-BP) suggested that it might serve as a target for NO produced in response to glutamatergic stimulation in neurons. In the present study, we demonstrate that N-methyl-D-aspartate, acting through NO, stimulates the RNA-binding function of the IRE-BP in brain slices while diminishing its aconitase activity. In addition, we demonstrate a selective localization of the IRE-BP in discrete neuronal structures, suggesting a potential role for this protein in the response of neurons to NO.