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PXD060814

PXD060814 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleLdm1 interaction proteomics of Ldm1-GFP cells
DescriptionOrganelle 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 factors that couple 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 ER, 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 actin/myosin-based cellular reorganization.
HostingRepositoryPRIDE
AnnounceDate2026-02-23
AnnouncementXMLSubmission_2026-02-23_02:48:05.854.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD060814
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterBianca Esch
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: NEWT:4932;
ModificationListacetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-02-14 04:30:30ID requested
12026-02-23 02:48:06announced
Publication List
10.6019/PXD060814;
10.1016/J.CELREP.2025.116475;
Keyword List
submitter keyword: QExactivePlus, affinity purification, S. cerevisiae,LC-MSMS
Contact List
Florian Fröhlich
contact affiliationBioanalytical Chemistry Section, Department of Biology/Chemistry, Osnabrück University, Germany
contact emailflorian.froehlich@uni-osnabrueck.de
lab head
Bianca Esch
contact affiliationOsnabrück University
contact emailbianca.esch@uos.de
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
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