Authors
Zhao XT, Diep DTV, Percifull L, Fausten RM, Hugenroth M, Höhne P, Leite B, Esch BM, Collado J, Keller J, Wilmes S, Turhan MA, Wälte M, Becker T, Kümmel D, Schuberth C, Fernández-Busnadiego R, Fröhlich F, Wedlich-Söldner R, Bohnert M
Journal
Cell Reports
Citation
Cell Rep. 2025 Oct 25;44(11):116475.
Abstract
Organelle motility enables strategic cellular reorganizations. In yeast, this process depends on the actin cytoskeleton, type V myosin motor proteins, and organelle-specific myosin adaptor proteins. While the myosin adaptors for most organelles are known, the coupling of myosin to lipid droplets (LDs), the cellular lipid storage organelles, remained enigmatic. Using genome-wide screening, we identified Ldm1 (lipid droplet motility 1/Yer085c) as a myosin adaptor. Ldm1 binds to the globular tail domain of the myosin Myo2 and to the LD surface protein Ldo16 to enable actin-dependent LD motility. Ldo16 has additional roles in LD contact sites to the vacuole and the endoplasmic reticulum, suggesting a coordination of LD motility and organelle tethering. Ldm1 has a second role in mitochondrial transport, and elevated Ldm1 levels rescue defects of the mitochondrial Myo2-adaptors Mmr1/Ypt11. Our work identifies the molecular machinery for LD motility and contributes to a comprehensive understanding of acto-myosin-based cellular reorganization.
