Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1864, Issue 11, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbagen.2020.129685
Keywords
Iron chaperone; PCBP; Cytosolic iron transport
Categories
Funding
- JSPS KAKENHI [19K23722, 20K07309, 20H05502]
- National Health and Medical Research Council of Australia [1159596, 1060482]
- National Breast Cancer Foundation of Australia [IIRS-19-048]
- Grants-in-Aid for Scientific Research [19K23722, 20H05502, 20K07309] Funding Source: KAKEN
- National Health and Medical Research Council of Australia [1060482, 1159596] Funding Source: NHMRC
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Background: Intracellular iron transport is mediated by iron chaperone proteins known as the poly(rC)-binding proteins (PCBPs), which were originally identified as RNA/DNA-binding molecules. Scope of review: PCBPs assume a role as not only as cytosolic iron carriers, but also as regulators of iron transport and recycling. PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1. Major conclusions: Both PCBP1 and PCBP2 possess iron-binding activity and form hetero/homo dimer complexes. These iron chaperones have a subset of non-redundant functions and regulate iron metabolism independently. General significance: This intracellular iron chaperone system mediated by PCBPs provide a transport gateway of ferrous iron that may potentially link with dynamic, inter-organelle interactions to safely traffic intracellular iron.
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