ArticleThe Journal of biological chemistry2013
IOP1 protein is an external component of the human cytosolic iron-sulfur cluster assembly (CIA) machinery and functions in the MMS19 protein-dependent CIA pathway.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 45 citations in OpenAlex.
- Regulatory networks of iron sulfur cluster biology in cancer mechanisms and therapeutic perspectives.iScience · 2026Review
- Nar1 binds the cytosolic iron sulfur cluster assembly targeting complex via a bipartite interaction interface.bioRxiv : the preprint server for biology · 2026Article
- NARFL Knockout Triggers Ferroptosis-Driven Vascular Endothelial Dysfunction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Control of Replication Stress Response by Cytosolic Fe-S Cluster Assembly (CIA) Machinery.Cells · 2025Review
- Maintenance of genome integrity by the late-acting cytoplasmic iron-sulfur assembly (CIA) complex.Frontiers in genetics · 2023Review
- Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021Review
- Iron-Sulfur Cluster Biogenesis as a Critical Target in Cancer.Antioxidants (Basel, Switzerland) · 2021Review
- Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism-Review.Molecules (Basel, Switzerland) · 2020Review
- CIAO3 protein forms a stable ternary complex with two key players of the human cytosolic iron-sulfur cluster assembly machinery.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Nubp2 is required for cranial neural crest survival in the mouse.Developmental biology · 2020Article
- Adaptation to life on land at high OProceedings. Biological sciences · 2019Article
- Branched late-steps of the cytosolic iron-sulphur cluster assembly machinery of Trypanosoma brucei.PLoS pathogens · 2018Article
- NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis.Molecules (Basel, Switzerland) · 2018Review
- Iron-sulfur cluster biosynthesis and trafficking - impact on human disease conditions.Metallomics : integrated biometal science · 2018Review
- Cellular requirements for iron-sulfur cluster insertion into the antiviral radical SAM protein viperin.The Journal of biological chemistry · 2017Article
- The CIA Targeting Complex Is Highly Regulated and Provides Two Distinct Binding Sites for Client Iron-Sulfur Proteins.Cell reports · 2017Article
- Article
- Emerging critical roles of Fe-S clusters in DNA replication and repair.Biochimica et biophysica acta · 2015Review
- Cell biology of disease: Telomeropathies: an emerging spectrum disorder.The Journal of cell biology · 2014Review
- Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron-sulfur proteins.Cell metabolism · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emerging link between iron metabolism and genome integrity is increasingly clear. Recent studies have revealed that MMS19 and cytosolic iron-sulfur cluster assembly (CIA) factors form a complex and have central roles in CIA pathway. However, the composition of the CIA complex, particularly the involvement of the Fe-S protein IOP1, is still unclear. The roles of each component are also largely unknown. Here, we show that MMS19, MIP18, and CIAO1 form a tight "core" complex and that IOP1 is an "external" component of this complex. Although IOP1 and the core complex form a complex both in vivo and in vitro, IOP1 behaves differently in vivo. A deficiency in any core component leads to down-regulation of all of the components. In contrast, IOP1 knockdown does not affect the level of any core component. In MMS19-overproducing cells, other core components are also up-regulated, but the protein level of IOP1 remains unchanged. IOP1 behaves like a target protein in the CIA reaction, like other Fe-S helicases, and the core complex may participate in the maturation process of IOP1. Alternatively, the core complex may catch and hold IOP1 when it becomes mature to prevent its degradation. In any case, IOP1 functions in the MMS19-dependent CIA pathway. We also reveal that MMS19 interacts with target proteins. MIP18 has a role to bridge MMS19 and CIAO1. CIAO1 also binds IOP1. Based on our in vivo and in vitro data, new models of the CIA machinery are proposed.
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