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Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson–Gilford progeria syndrome
TLDR
It is shown by light and electron microscopy that HGPS is associated with significant changes in nuclear shape, including lobulation of the nuclear envelope, thickening of thenuclear lamina, loss of peripheral heterochromatin, and clustering of nuclear pores. Expand
The nuclear lamina comes of age
TLDR
These complexes provide new insights into cell architecture, as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies — clinical disorders that range from Emery–Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson–Gilford progeria syndrome. Expand
Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes.
TLDR
Observations show that lmn-1 is an essential gene in C. elegans, and that the nuclear lamins are involved in chromatin organization, cell cycle progression, chromosome segregation, and correct spacing of NPCs. Expand
Nuclear lamins: building blocks of nuclear architecture.
TLDR
Experimental and genetic evidence suggest that nuclear lamins are involved in a number of other functions including nuclear envelope assembly, DNA synthesis, transcription, and apoptosis, and speculate about possible mechanisms through which mutations in lamins give rise to disease. Expand
Lamins: nuclear intermediate filament proteins with fundamental functions in nuclear mechanics and genome regulation.
TLDR
The lamin-based complexes and their specific functions provide insights into possible disease mechanisms for human laminopathies, ranging from muscular dystrophy to accelerated aging, as observed in Hutchinson-Gilford progeria and atypical Werner syndromes. Expand
Meiotic Chromosome Homology Search Involves Modifications of the Nuclear Envelope Protein Matefin/SUN-1
TLDR
The data suggest that the properties of the nuclear envelope are altered during the time window when homologs are sorted and Matefin/SUN-1 aggregates form, thereby controling the movement, homologous pairing and interhomolog recombination of chromosomes. Expand
Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death.
TLDR
CED-4 translocation induced by the cell-death activator EGL-1 was blocked by a gain-of-function mutation in cED-9 but was not dependent on ced-3 function, suggesting that CED- 4 translocation precedes caspase activation and the execution phase of programmed cell death. Expand
The nuclear envelope protein Matefin/SUN-1 is required for homologous pairing in C. elegans meiosis.
TLDR
The data on this mTF-1/sun-1 allele challenge the previously postulated role of the centrosome/spindle organizing center in chromosome pairing, and clearly support a role for MTF- 1/SUN-1 in meiotic chromosome reorganization and in homolog recognition. Expand
SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton
TLDR
It is proposed that SUN-domain proteins connect cytoplasmic and nucleoplasmic activities, by serving both as mechanical adaptors and nuclear envelope receptors, to physically connect the nucleus to every major component of the cytoskeleton. Expand
C. elegans nuclear envelope proteins emerin, MAN1, lamin, and nucleoporins reveal unique timing of nuclear envelope breakdown during mitosis.
TLDR
The timing of nuclear disassembly in C. elegans is novel and may reflect its evolutionary position between unicellular and more complex eukaryotes. Expand
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