@article {2925,
	title = {Filaments assembly of ectopically expressed Caenorhabditis elegans lamin within Xenopus oocytes.},
	journal = {J Struct Biol},
	volume = {177},
	number = {1},
	year = {2012},
	month = {2012 Jan},
	pages = {113-8},
	abstract = {Lamins are the major components of the nuclear lamina, a filamentous layer underlying the inner nuclear membrane and attached to the peripheral chromatin. Lamins are required for maintaining nuclear shape and are involved in most nuclear activities. Here, we studied the 3D organization of the nuclear lamina formed upon the expression of Caenorhabditis elegans lamin (Ce-lamin) within the nucleus of a Xenopus laevis oocyte. We show that Ce-lamin forms an intricate 3D meshwork of 5-6 nm lamin protofilaments. The diverse protofilament interactions and organization may shed light upon the unique mechano-elastic properties of the nuclear lamina scaffold supporting the nuclear envelope. The Q159K Hutchinson-Gilford Progeria Syndrome-linked mutation alters interactions between protofilaments within the lamina, leading to the formation of more bundled arrays of less isotropically-oriented protofilaments. Using this system, we show for the first time the organization of lamin proteins that were translated and assembled within the environment of a living cell.},
	keywords = {Animals, Caenorhabditis elegans, Cytoskeleton, Female, Gene Expression Regulation, Image Processing, Computer-Assisted, Lamins, Microscopy, Electron, Scanning, Nuclear Lamina, Oocytes, Protein Structure, Tertiary, Xenopus laevis},
	issn = {1095-8657},
	doi = {10.1016/j.jsb.2011.11.002},
	author = {Grossman, Einat and Dahan, Idit and Stick, Reimer and Goldberg, Martin W and Gruenbaum, Yosef and Medalia, Ohad}
}
