AI Article Synopsis
- MitoNEET, an iron-sulphur protein in the mitochondrial outer membrane, is linked to the drug pioglitazone but its exact molecular function remains unclear.
- Researchers identified a specific site for nitric oxide (NO) access to the mitoNEET's [2Fe-2S] cluster and found that both oxygen and pioglitazone can block this access.
- This discovery suggests a role for mitoNEET in mitochondrial signal transduction related to hypoxia, revealing new insights into how [Fe-S] clusters may function in signaling processes in eukaryotic cells.
Article Abstract
The mitochondrial outer membrane iron-sulphur ([Fe-S]) protein mitoNEET has been extensively studied as a target of the anti-inflammatory and type-2 diabetes drug pioglitazone and as a protein affecting mitochondrial respiratory rate. Despite these extensive past studies, its molecular function has yet to be discovered. Here, we applied an interdisciplinary approach and discovered an explicit nitric oxide (NO) access site to the mitoNEET [2Fe-2S] cluster. We found that O and pioglitazone block NO access to the cluster, suggesting a molecular function for the mitoNEET [2Fe-2S] cluster in mitochondrial signal transduction. Our discovery hints at a new pathway via which mitochondria can sense hypoxia through O protection of the mitoNEET [2Fe-2S] cluster, a new paradigm in understanding the importance of [Fe-S] clusters for gasotransmitter signal transduction in eukaryotes.
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| http://dx.doi.org/10.1002/1873-3468.15097 | DOI Listing |
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