Various neurological diseases are linked to changes in mitochondrial trafficking in axons. Thus, it is crucial to understand how dynamics of mitochondria are regulated on the molecular level. From a candidate screen, we identified SFXN-1.2 to regulate both morphologies as well as dynamics of mitochondria. SFXN-1.2 is an ortholog of human Sideroflexin 1/3 associated with Alzheimer's disease and Parkinson's diseases. We demonstrate that SFXN-1.2 binds to kinesin-3 KIF1A(UNC-104) via CX32 (Connexin 32 or GJB1), a protein known to be linked to Charcot-Marie-Tooth disease. While SFXN-1.2 and CX32 affect the dynamics of mitochondria, they also affect the motility of the molecular motor UNC-104 alone. From yeast two-hybrid, co-immunoprecipitation and bimolecular fluorescent complementation assays, we narrowed down critical interaction schemes of the UNC-104/CX32/SFXN-1.2 complex providing a complex molecular model.Interestingly, though UNC-104 binds to synaptic vesicles via its PH domain, we found no role of this domain in linking the motor to mitochondria. While UNC-104 trafficking is diminished in neurons of sfxn-1.2 mutants, motility of conventional kinesin-1 UNC-116 remains unaffected. Our data suggest that UNC-104 and UNC-116 act in parallel pathways likely co-transporting mitochondria. We also show that sfxn-1.2-induced changes in mitochondrial morphologies are independent of the fusion/fission machinery and that neither mitochondrial bioenergetics nor mitophagy are affected by sfxn-1.2 mutations. Strikingly, mutations in SFXN-1.2 lead to motor- and sensory neuron defects in C. elegansnegatively affecting the animal's touch responses as well as restricting body movements - pathological phenotypes commonly seen in neurological diseases.