Activation of a cryptic splice site at glycine-608 on one of these proteins is a cause of (*) Hutchinson-Gilford progeria.   
Mutation in a protein responsible for processing these proteins causes restrictive dermopathy in infants; that protein is the matrix metalloproteinase ZMPSTE24. An abnormal form of these proteins retains the farnesyl group on its C-terminus after processing. One isoform of these proteins interacts with emerin, mutations in which cause Emery-Dreifuss Muscular Dystrophy. The A and C types of these proteins are alternatively spliced from the same gene. Activation of a cryptic splice site at glycine-608 on one of these proteins is a cause of (*) Hutchinson-Gilford progeria.   These proteins' rod domains bind to S/MAR regions, which contain AT-rich patches. These proteins are phosphorylated by MPF during the cell cycle in order to disassemble a certain organelle.  For 10 points, name these intermediate filaments that form a meshwork on the inner surface of the nucleus.
Mutation in a protein responsible for processing these proteins causes restrictive dermopathy in infants; that protein is the matrix metalloproteinase ZMPSTE24.
nuclear lamins [prompt on “intermediate filaments”, “nuclear lamina”, “nuclear matrix”]