Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms

• Published in: Nature (London) Vol. 586; no. 7831; pp. 807 - 811
• Main Authors: Billesbølle, Christian B., Azumaya, Caleigh M., Kretsch, Rachael C., Powers, Alexander S., Gonen, Shane, Schneider, Simon, Arvedson, Tara, Dror, Ron O., Cheng, Yifan, Manglik, Aashish
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 29.10.2020; Nature Publishing Group
• Subjects: 101/1; 101/28; 14; 631/45/321/1155; 631/45/612/1237; 631/45/776; 631/535/1258/1259; 96/95; Analysis; Apoproteins - chemistry; Apoproteins - metabolism; Apoproteins - ultrastructure; Binding Sites; Cation Transport Proteins - chemistry; Cation Transport Proteins - metabolism; Cation Transport Proteins - ultrastructure; Cobalt; Cobalt - chemistry; Cobalt - metabolism; Cryoelectron Microscopy; Degradation; Domains; Efflux; Electron microscopy; Hepcidin; Hepcidins - chemistry; Hepcidins - metabolism; Homeostasis; Humanities and Social Sciences; Humans; Internalization; Iron; Iron - chemistry; Iron - metabolism; Iron in the body; Iron proteins; Lipids; Membrane proteins; Microscopy; Molecular dynamics; Molecular Dynamics Simulation; multidisciplinary; Mutation; Protein Domains; Protein turnover; Proteolysis; Science; Science (multidisciplinary); Structure; Structure-function relationships; United States

The serum level of iron in humans is tightly controlled by the action of the hormone hepcidin on the iron efflux transporter ferroportin. Hepcidin regulates iron absorption and recycling by inducing the internalization and degradation of ferroportin 1 . Aberrant ferroportin activity can lead to dise...