Neutrophils require energy supplied by mitochondria oxidative phosphorylation (OXPHOS) during chemotaxis, whereas the energy of neutrophil depends on glycolysis under normal condition. However, it is unknown the mechanism in which the energy supply changes from glycolysis to OXPHOS. Leucine-rich repeat kinase 2 (LRRK2) is partially present in the mitochondrial outer membrane fraction. Lrrk2 deficient cells show mitochondrial fragmentation and reduction of OXPHOS activity. We previously reported that mitofusin 2 (Mfn2) knockdown by shRNA suppressed mitochondrial morphological changes, OXPHOS activation and chemotactic activity upon fMLP stimulation in differentiated HL-60 (dHL-60) cells. Here, we investigated whether LRRK2, which is reported to bind to MFN2, is involved in neutrophils chemotaxis. Mouse Lrrk2 knockout neutrophils showed reduction of chemotactic activity. LRRK2 knockdown in dHL-60 cells showed reduction of chemotactic activity, OXPHOS activation, GTP binding activity of MFN2, and suppression of mitochondrial morphological changes upon fMLP stimulation. Furthermore, LRRK2 kinase inhibitor MLi-2 resulted in an increase in chemotactic activity. These results suggested that LRRK2 is involved in chemotaxis of neutrophils, and that LRRK2 kinase activity in particular is important for chemotaxis.