Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Each member of the poly-r(C)-binding protein 1 (PCBP) family exhibits iron chaperone activity toward ferritin.

Leidgens S, Bullough KZ, Shi H, Li F, Shakoury-Elizeh M, Yabe T, Subramanian P, Hsu E, Natarajan N, Nandal A, Stemmler TL, Philpott CC

The mechanisms through which iron-dependent enzymes receive their metal cofactors are largely unknown. Poly r(C)-binding protein 1 (PCBP1) is an iron chaperone for ferritin; both PCBP1 and its paralog PCBP2 are required for iron delivery to the prolyl hydroxylase that regulates HIF1. Here we show that PCBP2 is also an iron chaperone for ferritin. Co-expression of PCBP2 and human ferritins ... [more]

J. Biol. Chem. Jun. 14, 2013; 288(24);17791-802 [Pubmed: 23640898]

Throughput

  • Low Throughput

Additional Notes

  • Figure 4
  • isothermal titration calorimetry, iron present
  • source of ferritin is equine

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
FTH1 PCBP1
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
1113134

Curated By

  • BioGRID