{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Ding X"],"funding":["NIGMS NIH HHS"],"pubmed_abstract":["Emery-Dreifuss muscular dystrophy (EDMD) arises from mutations in nuclear lamins or emerin. Current pathological models emphasize defects in nuclear mechanics and transcription regulation. Yet these models do not fully explain the complexity of EDMD or other laminopathies. Here, we uncover an emerging pathway linking nuclear lamina defects to the reorganization of cytoplasmic biophysics, revealing how nuclear dysfunction cascades throughout the cell. Using <i>Caenorhabditis elegans</i> EDMD models, we demonstrate that lamin mutations dramatically alter cytoplasmic organization, reducing macromolecular crowding and increasing diffusivity of 40 nm G enetically E ncoded M ultimeric (GEM) nanoparticles. These striking biophysical changes coincide with nuclear positioning defects and collapsed "],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.09.22.677926"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12485773"],"repository":["biostudies-literature"],"pubmed_title":["Muscular dystrophy-associated lamin variants disrupt cellular organization through a nucleolar-ribosomal axis controlling cytoplasmic macromolecular crowding."],"pmcid":["PMC12485773"],"funding_grant_id":["R35 GM134859"],"pubmed_authors":["Luxton GWG","Ding X","Kumari S","Gregory E","Starr DA"],"additional_accession":[]},"is_claimable":false,"name":"Muscular dystrophy-associated lamin variants disrupt cellular organization through a nucleolar-ribosomal axis controlling cytoplasmic macromolecular crowding.","description":"Emery-Dreifuss muscular dystrophy (EDMD) arises from mutations in nuclear lamins or emerin. Current pathological models emphasize defects in nuclear mechanics and transcription regulation. Yet these models do not fully explain the complexity of EDMD or other laminopathies. Here, we uncover an emerging pathway linking nuclear lamina defects to the reorganization of cytoplasmic biophysics, revealing how nuclear dysfunction cascades throughout the cell. Using <i>Caenorhabditis elegans</i> EDMD models, we demonstrate that lamin mutations dramatically alter cytoplasmic organization, reducing macromolecular crowding and increasing diffusivity of 40 nm G enetically E ncoded M ultimeric (GEM) nanoparticles. These striking biophysical changes coincide with nuclear positioning defects and collapsed ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-05-07T03:21:59.645Z","creation":"2026-05-07T03:12:48.365Z"},"accession":"S-EPMC12485773","cross_references":{"pubmed":["41040396"],"doi":["10.1101/2025.09.22.677926"]}}