Progerin (UniProt# P02545-6) is a truncated version of the lamin Aprotein involved in the pathology of Hutchinson–Gilford progeria syndrome. Progerin is most often generated by a sporadic single point nucleotide polymorphism c.1824 C>T (GGC -> GGT, p.Gly608Gly) in the gene that codes for matured Lamin A.[1] This mutation activates a cryptic splice site that induces a larger mutation in the processed prelamin A messenger RNA, causing the deletion of a 50 amino-acid group near the C-terminus of the prelamin A protein.[2] The endopeptidase ZMPSTE24 cannot cleave between the missing RSY - LLG amino acid sequence (as seen in the figure) during the maturation of Lamin A, due to the deletion of the 50 amino acids which included that sequence. This leaves the intact premature Lamin A bonded to the methylated carboxyl farnesyl group creating the defective protein Progerin, rather than the desired protein matured Lamin A. Approximately 90% of all Hutchinson–Gilford progeria syndrome cases are heterozygous for this deleterious single nucleotide polymorphism within exon 11 of the LMNA gene causing the post-translational modifications to produce progerin.[3]
Lamin A constitutes a major structural component of the lamina, a scaffold of proteins found inside the nuclear membrane of a cell; progerin does not properly integrate into the lamina, which disrupts the scaffold structure and leads to significant disfigurement of the nucleus, characterized by a globular shape.[4] Progerin activates genes that regulate stem celldifferentiation via the Notch signaling pathway.[5] Progerin increases the frequency of unrepaired double-strand breaks in DNA following exposure to ionizing radiation.[6] Also, overexpression of progerin is correlated with an increase in non-homologous end joining relative to homologous recombination among those DNA double-strand breaks that are repaired.[7] Furthermore, the fraction of homologous recombination events occurring by gene conversion is increased. These findings suggest that the normal untruncated nuclear lamina has an important role in the proper repair of DNA double-strand breaks.[6]
^Gordon, Leslie B.; Brown, W. Ted; Collins, Francis S. (1993), Adam, Margaret P.; Ardinger, Holly H.; Pagon, Roberta A.; Wallace, Stephanie E. (eds.), "Hutchinson-Gilford Progeria Syndrome", GeneReviews®, Seattle (WA): University of Washington, Seattle, PMID20301300, retrieved 2022-04-26