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

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.

SUBMITTER: Philpott CC

PROVIDER: S-EPMC7484093 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

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

Philpott Caroline C CC Patel Sarju J SJ Protchenko Olga O

Biochimica et biophysica acta. Molecular cell research 20200821 11

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 ...[more]

PMID: 32835748

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