Iron-sulfur cluster co-chaperone protein HscB, mitochondrial (HSCB)

Iron-sulfur cluster co-chaperone protein HscB, mitochondrial (HSCB) is a J-domain co-chaperone of the Hsp40 family that is essential for mitochondrial iron-sulfur (Fe–S) cluster biosynthesis[3][5]. HSCB interacts with the scaffold protein ISCU to facilitate Fe–S cluster transfer within a multiprotein system involving HSPA9 (mortalin/mitochondrial Hsp70) and other biogenesis factors[3][5][1]. Primarily, HSCB mediates protein-protein interactions required for stabilization, maturation, and delivery of Fe–S clusters—which are vital cofactors for respiratory chain complexes and other mitochondrial enzymes[2][5]. Deficiency or mutation in HSCB results in defects in mitochondrial function, leading to diseases such as sideroblastic anemia and potentially neurodegenerative conditions linked to impaired iron metabolism[3][6]. There are currently no approved drugs targeting HSCB directly.

Other names

Iron-sulfur cluster co-chaperone protein HscB, cytoplasmicJ-type co-chaperone HSC20DnaJ homolog subfamily C member 20DNAJC20Jac1SIDBA5HSC20JAC1