Hutchinson-Gilford progeria syndrome (HGPS, OMIM 176670) is a rare premature 
aging disorder that leads to death at an average age of 14.7 years due to 
myocardial infarction or stroke. The most common mutation in HGPS is at position 
G608G (GGC>GGT) within exon 11 of the LMNA gene. This mutation results in the 
deletion of 50 amino acids at the carboxyl-terminal tail of prelamin A, 
producing a truncated farnesylated protein called progerin. Lamins play 
important roles in the organization and structure of the nucleus. The nuclear 
build-up of progerin causes severe morphological and functional changes in 
interphase HGPS cells. In this study, we investigated whether progerin elicits 
spatiotemporal deviations in mitotic processes in HGPS fibroblasts. We analyzed 
the nuclear distribution of endogenous progerin during mitosis in relation to 
components of the nuclear lamina, nuclear envelope (NE) and nuclear pores. We 
found that progerin caused defects in chromosome segregation as early as 
metaphase, delayed NE reformation and trapped lamina components and inner NE 
proteins in the endoplasmic reticulum at the end of mitosis. Progerin displaced 
the centromere protein F (CENP-F) from metaphase chromosome kinetochores, which 
caused increased chromatin lagging, binucleated cells and genomic instability. 
This accumulation of progerin-dependent defects with each round of mitosis 
predisposes cells to premature senescence.