The Myo2 adaptor Ldm1 and its receptor Ldo16 mediate actin-dependent lipid droplet motility

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.

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Publication Details

Journal
Cell Reports
Published
2025-10-25
DOI
https://doi.org/10.1016/j.celrep.2025.116475
Citations
2
Primary Topic
Nuclear Structure and Function
Type
article
Field-Weighted Citation Impact
1.61
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article

The Myo2 adaptor Ldm1 and its receptor Ldo16 mediate actin-dependent lipid droplet motility

Barbara R. Leite, Javier Collado, Mike Wälte, Christian Schuberth et al.
2 citations
Cell Reports
Nuclear Structure and Function
1.61
article

The Myo2 adaptor Ldm1 and its receptor Ldo16 mediate actin-dependent lipid droplet motility

Barbara R. Leite, Javier Collado, Mike Wälte, Christian Schuberth, Marie Hugenroth, Meryem Aysenur Turhan, Jenny Keller, Duy Trong Vien Diep, Roland Wedlich‐Söldner, Rubén Fernández‐Busnadiego, Thomas Becker, Daniel Kümmel, Florian Fröhlich, Rebecca Martina Fausten, Maria Bohnert, Bianca M. Esch, Stephan Wilmes, Pascal Höhne, Louis Percifull, Xue-Tong Zhao
article en
2 citations

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.

Cell ReportsVol. 44(11)
University of Bonn (DE), Osnabrück University (DE), University of Münster (DE), Universitätsmedizin Göttingen (DE), FH Münster University of Applied Sciences (DE), University of Göttingen (DE)
Openalex Percentile: Top 14%
Nuclear Structure and Function
1.61
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