Management versus miscues in the cytosolic labile iron pool: The varied functions of iron chaperones

Biochim Biophys Acta Mol Cell Res. 2020 Nov;1867(11):118830. doi: 10.1016/j.bbamcr.2020.118830. Epub 2020 Aug 21.

Abstract

Iron-containing proteins rely on the incorporation of a set of iron cofactors for activity. The cofactors must be synthesized or assembled from raw materials located within the cell. The chemical nature of this pool of raw material - referred to as the labile iron pool - has become clearer with the identification of micro- and macro-molecules that coordinate iron within the cell. These molecules function as a buffer system for the management of intracellular iron and are the focus of this review, with emphasis on the major iron chaperone protein coordinating the labile iron pool: poly C-binding protein 1.

Keywords: Ferroptosis; Glutathione; Iron chaperone; PCBP; Steatosis.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Cytosol / metabolism
  • DNA-Binding Proteins / genetics*
  • Fatty Liver / genetics
  • Fatty Liver / pathology
  • Ferroptosis / genetics
  • Glutathione / genetics
  • Glutathione / metabolism
  • Humans
  • Iron / metabolism*
  • Iron-Sulfur Proteins / genetics*
  • Iron-Sulfur Proteins / metabolism
  • Molecular Chaperones / genetics*
  • RNA-Binding Proteins / genetics*

Substances

  • DNA-Binding Proteins
  • Iron-Sulfur Proteins
  • Molecular Chaperones
  • PCBP1 protein, human
  • RNA-Binding Proteins
  • Iron
  • Glutathione