@article {2982,
	title = {Fate of the nuclear lamina during Caenorhabditis elegans apoptosis.},
	journal = {J Struct Biol},
	volume = {137},
	number = {1-2},
	year = {2002},
	month = {2002 Jan-Feb},
	pages = {146-53},
	abstract = {Invertebrates and in Drosophila, lamins and lamin-associated proteins are primary targets for cleavage by caspases. Eliminating mammalian lamins causes apoptosis, whereas expressing mutant lamins that cannot be cleaved by caspase-6 delay apoptosis. Caenorhabditis elegans has a single lamin protein, Ce-lamin, and a caspase, CED-3, that is responsible for most if not all somatic apoptosis. In this study we show that in C. elegans embryos induced to undergo apoptosis Ce-lamin is degraded surprisingly late. In such embryos CED-4 translocated to the nuclear envelope but the cytological localization of Ce-lamin remained similar to that in wild-type embryos. TUNEL labeling indicated that Ce-lamin was degraded only after DNA is fragmented. Ce-lamin, Ce-emerin, or Ce-MAN1 were not cleaved by recombinant CED-3, showing that these lamina proteins are not substrates for CED-3 cleavage. These results suggest that lamin cleavage probably is not essential for apoptosis in C. elegans.},
	keywords = {Animals, Apoptosis, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Caspases, Cell Nucleus, Fluorescent Antibody Technique, Indirect, In Situ Nick-End Labeling, Lamins, Membrane Proteins, Nuclear Lamina, Nuclear Proteins, Plasmids, Protein Binding},
	issn = {1047-8477},
	doi = {10.1006/jsbi.2002.4452},
	author = {Tzur, Yonatan B and Hersh, Bradley M and Horvitz, H Robert and Gruenbaum, Yosef}
}
