ABCB7 is a mitochondrial ATP-binding cassette transporter that exports glutathione-coordinated iron-sulfur clusters, such as [2Fe-2S]-(GS)₄, from the mitochondria to the cytosol in an ATP-dependent manner, enabling assembly of cytosolic iron-sulfur cluster-containing proteins. The transporter also participates in cellular iron homeostasis through functional interactions with FECH and ABCB10, and regulates heme biosynthesis and mitochondrial function. In cardiomyocytes, ABCB7 modulates cellular reactive oxygen species levels through its interaction with COX4I1. Dysfunction of ABCB7 underlies X-linked sideroblastic anemia with cerebellar ataxia (XLSA/A), where reduced iron-sulfur cluster export impairs ALAS2 translation and heme synthesis 1. In myelodysplastic syndromes with ring sideroblasts (MDS-RS), somatic SF3B1 mutations cause ABCB7 missplicing and downregulation, leading to mitochondrial iron accumulation 2. Loss of ABCB7 is synthetic lethal to copper ionophores—UM4118, a copper ionophore under investigation, shows heightened activity in SF3B1-mutated acute myeloid leukemia (AML) samples, with ABCB7 loss enhancing copper-mediated cuproptosis 3. In esophageal cancer, ABCB7 is upregulated and promotes cell survival by suppressing both apoptotic and non-apoptotic cell death through control of mitochondrial ROS and HIF1α-driven NF-κB signaling 4. These findings position ABCB7 modulation as a potential therapeutic strategy in SF3B1-mutated leukemias and select solid tumors.