Abstract
The linker of nucleoskeleton and cytoskeleton (LINC) is the primary node of force transduction at the nucleus - essential for regulating its morphology and position in mammalian cells. LINC spans both nucleus membranes; interacting with the nuclear lamina and chromatin within the nucleus, whilst also interacting with cytoskeletal filaments in the cytoplasm. Dysregulation of LINC and its interactions underlies numerous laminopathies with diverse manifestations, including deafness, muscular dystrophy and developmental disorders. Although a wealth of genetics and cell biology has described its large network of interactions, its architecture and mechanism of assembly is largely unknown. We present an approach to understand this interaction using cryo-focused ion beam milling (FIB-milling) and cryo-electron tomography (cryo-ET). By promoting actin polymerisation in the cytoplasm, we have determined the structure and architecture of actin in the vicinity of the nucleus. By visualizing LINC and actin in its native environment, our results shed new light on the role of actin-LINC in nucleus morphology and positioning.
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