ABCB10 protein forms homodimers and homo-oligomers [7] that localize
into the inner mitochondrial membrane with nucleotide binding
domain (NBD) oriented to the mitochondrial matrix, suggesting its potential
role in the export of molecules out of mitochondria. The crystal
structure of ABCB10 revealed that overall fold of this protein is similar
to other eukaryotic ABC transporters [8]. While enhanced ABCB10 expression
in erythroid tissue suggested a functional role in differentiation
and/or function of this lineage, for several years this role remained elusive
and somewhat contentious. Murine Abcb10 was found to specifically
interact with mitoferrin-1 and ferrochelatase proteins during
erythroid maturation in haematopoietic tissues [9,10]. Recent data
using mouse Abcb10 KO model showed that Abcb10 is crucial for red
blood cell differentiation in vivo [11]. Interestingly, Abcb10 KO mice develop
similar severe manifestations to the Gata-1 KO mice [12],
confirming previous results of potential interplay between these two
genes. Using shRNA-mediated ABCB10 silencing in K562 cells,
Tang et al. [13] were able to show that ABCB10 is also required for
hemoglobinization and efficient red blood differentiation in a human
system