Title : The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.

Pub. Date : 2017 Aug 11

PMID : 28655775






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Heme poly(rC) binding protein 2 Homo sapiens
2 In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Heme poly(rC) binding protein 2 Homo sapiens
3 Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1. Heme poly(rC) binding protein 2 Homo sapiens
4 These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon. Heme poly(rC) binding protein 2 Homo sapiens