Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence.
Specificity
Natural and recombinant Mouse Prelamin-A/C
Subcellular Location
Nucleus Nucleus envelope Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C.
Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Proteolytically processed isoform A interacts with NARF (By similarity). Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Prelamin-A/C interacts with EMD (By similarity). Interacts with MLIP; may regulate MLIP localization to the nucleus envelope.