ArticleMolecular biology of the cell2014
The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to transfer forces from the cytoplasm to the nucleoskeleton during nuclear migration.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 70 citations in OpenAlex.
- Nuclei on the move: LINC complex-dependent and -independent mechanisms of nuclear migration in development.Nucleus (Austin, Tex.) · 2026Review
- Muscular dystrophy-associated lamin variants disrupt cellular organization through a nucleolar-ribosomal axis.Science advances · 2026Article
- Arabidopsis KASH domains are differentially required for distinct LINC complex roles in stomata, roots and pollen.Journal of cell science · 2026Article
- Vascular Mechanobiology: From Membrane to Nucleus.Advances in experimental medicine and biology · 2026Review
- The KASH protein UNC-83 differentially regulates kinesin-1 activity to control developmental stage-specific nuclear migration.Current biology : CB · 2025Article
- The Pea Inner Nuclear Membrane SUN Domain Protein Modulates Plant (a)biotic Stress Responses by Regulating Nuclear Dynamics.Molecular plant pathology · 2025Article
- Muscular dystrophy-associated lamin variants disrupt cellular organization through a nucleolar-ribosomal axis controlling cytoplasmic macromolecular crowding.bioRxiv : the preprint server for biology · 2025Article
- Nuclear deformability depends on H3K9-methylated heterochromatin anchorage to the nuclear periphery in Caenorhabditis elegans.Genetics · 2025Article
- Nuclear Envelope Dynamics inCells · 2025Review
- Review
- Article
- Anchorage of H3K9-methylated heterochromatin to the nuclear periphery helps mediate P-cell nuclear migration though constricted spaces inbioRxiv : the preprint server for biology · 2024Article
- Nuclear envelope assembly relies on CHMP-7 in the absence of BAF-LEM-mediated hole closure.Journal of cell science · 2023Article
- FLN-2 functions in parallel to LINC complexes and Cdc42/actin pathways during P-cell nuclear migration through constricted spaces inbioRxiv : the preprint server for biology · 2023Article
- Cellular and Genomic Features of Muscle Differentiation from Isogenic Fibroblasts and Myoblasts.Cells · 2023Article
- Caenorhabditis elegans models for striated muscle disorders caused by missense variants of human LMNA.PLoS genetics · 2023Article
- A humanized Caenorhabditis elegans model of hereditary spastic paraplegia-associated variants in KLC4.Disease models & mechanisms · 2023Article
- A cooperative network at the nuclear envelope counteracts LINC-mediated forces during oogenesis inScience advances · 2023Article
- Nuclear envelope assembly relies on CHMP-7 in the absence of BAF-LEM-mediated hole closure.bioRxiv : the preprint server for biology · 2023Article
- A humanizedbioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Nuclear migration is a critical component of many cellular and developmental processes. The nuclear envelope forms a barrier between the cytoplasm, where mechanical forces are generated, and the nucleoskeleton. The LINC complex consists of KASH proteins in the outer nuclear membrane and SUN proteins in the inner nuclear membrane that bridge the nuclear envelope. How forces are transferred from the LINC complex to the nucleoskeleton is poorly understood. The Caenorhabditis elegans lamin, LMN-1, is required for nuclear migration and interacts with the nucleoplasmic domain of the SUN protein UNC-84. This interaction is weakened by the unc-84(P91S) missense mutation. These mutant nuclei have an intermediate nuclear migration defect-live imaging of nuclei or LMN-1::GFP shows that many nuclei migrate normally, others initiate migration before subsequently failing, and others fail to begin migration. At least one other component of the nucleoskeleton, the NET5/Samp1/Ima1 homologue SAMP-1, plays a role in nuclear migration. We propose a nut-and-bolt model to explain how forces are dissipated across the nuclear envelope during nuclear migration. In this model, SUN/KASH bridges serve as bolts through the nuclear envelope, and nucleoskeleton components LMN-1 and SAMP-1 act as both nuts and washers on the inside of the nucleus.
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Registered trials
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