CDGSH Iron Sulfur Domain 1 Proteins (CISD1)

Human CDGSH Iron Sulfur Domain 1 (CISD1) interaction partners

1. The [2Fe-2S] clusters of mitoNEET are reduced via the formation of a transient complex that brings the [2Fe-2S] clusters of mitoNEET close to the redox-active [2Fe-2S] cluster of anamorsin.

2. The results suggest that flavin nucleotides may act as electron shuttles to reduce the mitoNEET [2Fe-2S] clusters and regulate mitochondrial functions in human cells.

3. Data suggest that, compared with oxygen, ubiquinone-2 is more efficient in oxidizing mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of reduced mitoNEET [2Fe-2S] clusters in mitochondrial outer membrane.

4. CISD1 inhibits ferroptosis by protecting the cells against mitochondrial lipid peroxidation.

5. the redox-sensing function of mNT is a key component of the cellular adaptive response to help stress-sensitive Fe-S proteins recover from oxidative injury.

6. A possible role of CISD1 in obesity-associated dysfunctional adipogenesis in human visceral adipose tissue.

7. Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process.

8. Glutathione reductase reduces mitochondrial protein mitoNEET [2Fe-2S] clusters.

9. Studies indicate that NEET proteins are associated with diseases including cancer and diabetes.

10. SNPs in three genes CYP26B1 rs2241057, CISD1 rs2251039, rs2590370, and TBX1 rs4819522 were involved in six potential pathways to influence serum prostate-specific antigen levels.

11. In this review, we evaluate the current understanding regarding how mitoNEET regulates cellular bioenergetics as well as the structural requirements for drug compound association with mitoNEET

12. MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/IRP1.

13. pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein.

14. The MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator.

15. Data show that the protein levels of NAF-1 (CISD2) and mNT (CISD1) are elevated in human epithelial breast cancer cells.

16. a loop (L2) 20 A away from the metal center exerts allosteric control over the cluster binding domain and regulates multiple properties of the metal center. Mutagenesis of L2 results in significant shifts in the redox potential of the [2Fe-2S] cluster.

17. NADPH can regulate both mitoNEET [2Fe-2S] cluster levels in the cell as well as the ability of the protein to transfer [2Fe-2S] clusters to cytosolic or mitochondrial acceptors.

18. These findings suggest a likely role for mNT in [2Fe-2S] and/or iron transfer to acceptor proteins.

19. crystal structure of H87C mitoNEET was determined to 1.7 A resolution (R factor = 18%) to investigate the structural basis of the changes in the properties of the 2Fe-2S cluster

20. The iron-sulfur cluster-containing protein mitoNEET interacts with two potentially redox active substances at the surface of mitochondria; mitoNEET forms complexes with resveratrol-3-sulfate, a primary metabolite of the natural product resveratrol.

Mouse (Murine) CDGSH Iron Sulfur Domain 1 (CISD1) interaction partners

1. mNEET plays a specific role in the formation of intermitochondrial junctions and thus participates in the adaptation of cells to physiological changes and to the control of mitochondrial homeostasis.

2. Together, these data suggest that mitoNEET KO mice exhibit many of the characteristics of early neurodegeneration in PD and may provide a novel drug discovery platform to evaluate compounds for enhancing mitochondrial function in neurodegenerative disorders.

3. mitoNEET protects intact cardiac cells from oxidative stress induced apoptosis during hypoxia and reoxygenation.

4. The elevation in circulating levels of adiponectin and Fgf15 led to normalized hepatic and serum levels of bile acids, limited hepatic accumulation of toxic bile, attenuated inflammation, and amelioration of liver injury in the ethanol-fed mNT knockout mice.

5. the mitoNEET-enriched fat pads feature a more vascularized, anti-inflammatory and less fibrotic environment.

6. The MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator.

7. study found that overexpression of mitoNEET enhances lipid uptake and storage, leading to an expansion of the mass of adipose tissue

8. mitoNEET is located in mitochondrial fraction of adipocytes.

9. mito- NEET is an important iron-containing protein involved in the control of maximal mitochondrial respiratory rates

Cow (Bovine) CDGSH Iron Sulfur Domain 1 (CISD1) interaction partners

1. mitoNEET is located in the mitochondrial fraction of bovine brain.