Publications by authors named "Eric S Hanson"
HOIL-1 is not required for iron-mediated IRP2 degradation in HEK293 cells.
Biochim Biophys Acta
February 2008
Iron regulatory protein 2 (IRP2) binds to iron-responsive elements (IREs) to regulate the translation and stability of mRNAs encoding several proteins involved in mammalian iron homeostasis. Increases in cellular iron stimulate the polyubiquitylation and proteasomal degradation of IRP2. One study has suggested that haem-oxidized IRP2 ubiquitin ligase-1 (HOIL-1) binds to a unique 73-amino acid (aa) domain in IRP2 in an iron-dependent manner to regulate IRP2 polyubiquitylation and degradation.
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- IRP2 plays a key role in managing iron levels in cells by regulating mRNAs that control iron uptake and storage.
- Iron triggers the rapid degradation of IRP2, while conditions like hypoxia and certain chemicals stabilize the protein against degradation.
- Research indicates that a 73-amino acid region of IRP2 isn’t essential for its degradation, and that iron-mediated IRP2 degradation is influenced by 2-oxoglutarate-dependent dioxygenases, suggesting a complex interaction between oxygen, iron, and IRP2 stability.