Function
CIAPIN1 is a key component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery, essential for the maturation of extramitochondrial Fe-S proteins. It participates in an electron transfer chain, playing a crucial role in an early step of cytosolic Fe-S biogenesis. This process involves facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. Notably, the NDOR1-CIAPIN1 complex is also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), likely by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. Beyond its role in Fe-S cluster assembly, CIAPIN1 exhibits anti-apoptotic effects within the cell. It participates in the negative regulation of cell death upon cytokine withdrawal. Moreover, CIAPIN1 promotes the development of hematopoietic cells.