“…Some new concepts have been published, based on the interaction of lamins with a wide spectrum of diverse proteins and on the mechanism by which lamin defects might alter these interactions to cause disease. Lamins not only interact with each other but also interact and modulate function or determine the location of key proteins of the nuclear membranes (emerin, nesprin, LBR, LAP, MAN1), LINC complex (SUN proteins), nuclear pore complex proteins (Nup153, Nup53), transcription factors (SREBP1, MOK2, pRb, c-Fos, Oct-1), nucleoplasmic proteins (BAF, LAP2α), proteins associated with signal transduction pathways (PKCα, PP1, PP2), DNA and chromatin (H2A, H2B histone dimers, heterochromatin protein-1) [for a review see 63,121]. It should be considered that the formation of a definite complex must be directed by different signaling events.…”