Abstract
The nucleoskeleton is primarily composed of intermediate type V filaments, which consist of lamin proteins. Human cells encode three genes for two types of lamins: the A-type lamins, primarily lamins A and C, which are products of alternative splicing of the LMNA gene; and the B-type lamins, lamin B1 and lamin B2, which are encoded by two separate genes (Gruenbaum et al., 2005). Lamin filaments assemble into homopolymers and mostly separate networks (Delbarre et al., 2006; Furukawa et al., 2009; Moir et al., 2000). B-type lamins are ubiquitously expressed in metazoan cells and are essential to cell survival (Harborth et al., 2001) because of the fundamental roles of lamin B proteins in transcription and other cellular signaling pathways. For example, lamin B1 is essential for RNA synthesis, and activity of RNA polymerases I and II (Tang et al., 2008). However, loss of lamin B1 in mouse embryonic fibroblasts does not result in any of the nuclear softening and cytoskeletal defects that are seen when lamin A is lost (Lammerding et al., 2006). Recently, lamin B2 has been shown to be required for nuclear migration in neurons (Coffinier et al., 2010).

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