[HTML][HTML] Management versus miscues in the cytosolic labile iron pool: The varied functions of iron chaperones
CC Philpott, SJ Patel, O Protchenko - Biochimica et Biophysica Acta (BBA) …, 2020 - Elsevier
CC Philpott, SJ Patel, O Protchenko
Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 2020•ElsevierIron-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 …
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 …
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.
Elsevier