SF3B1 and the riddle of the ring sideroblast

摘要

Other explanations should be considered. The absence of frameshift, nonsense, and splice-site mutations, the lack of key structural amino acid residues as sites for mutation, and the fact that the mutations are less deleterious than expected on the basis of chance all suggest that the mutated SF3B1 protein is likely to retain structural integrity, albeit with presumably altered function.3 Such altered function may either compromise a hitherto unknown physiologic role of SF3B1 in mitochondrial iron metabolism, or create a novel, unphysiologic effect on mitochondrial iron handling. SF3B1 does have functions unrelated to the splicing complex.