Iron-sulphur (Fe-S) clusters are small inorganic co-factors found in many proteins that have a variety of roles. It is now known that Fe-S clusters are also important in the maintenance of genome stability. The cytosolic iron-sulfur protein assembly (CIA) machinery, which facilitates Fe-S cluster insertion, is thought to cause genomic instability when downregulated, mainly through the simultaneous inactivation of multiple DNA repair pathways. Many Fe-S proteins involved in these pathways have already been identified, including DNA polymerases and helicases, but it is likely that many more proteins remain to be identified. Here, Roland Lill, Shay Ben-Aroya and colleagues (Ben-Shimon et al., 2018) investigate a link between Fe-S metabolism and spindle assembly and cell division. The authors first demonstrate that CIA2B and MMS19, two components of the CIA targeting complex, colocalise with components of the mitotic machinery, and downregulation of CIA2B and MMS19 impairs the mitotic cycle. Next, the authors demonstrate that the chromosome-associated kinesin KIF4A colocalises and physically interacts with the CIA targeting complex. They characterise a conserved cysteine-rich domain (CRD) at the C-terminus of KIF4A as a Fe-S cluster-binding site, and show that this domain can bind a Fe-S cluster when expressed in yeast or as a recombinant protein. Furthermore, the mitosis-related phenotypes obtained when removing the KIF4A CRD are the result of impaired Fe-S cluster binding. These findings demonstrate an important role of Fe-S cluster binding for the function and localisation of a mitotic kinesin.