Leishmanolysin Like Protein (LMLN)

McHugh et al. (2004) characterized invadolysin, the Drosophila ortholog of Leishmanolysin-like (LMLN), and showed that it is required for many aspects of mitosis including spindle assembly, nuclear envelope dynamics, and chromosome architecture. LMLN encodes a metalloprotease conserved among higher eukaryotes. Conservation of 14 cysteines and a zinc-metalloprotease motif among LMLN orthologs suggested structural similarity to leishmanolysin, a cell surface protein of the parasite Leishmania major required for pathogenesis. In stationary  cultured macrophages, human LMLN localizes to punctate or ring-like cytoplasmic structures but relocalizes to the leading edge of migratory cells. Mutation of Drosophila Lmln caused germ cell migration defects. The authors demonstrated that Drosophila Lmln cleaves lamin in vitro.