Emerin-prelamin A interplay in human fibroblasts

Cristina Capanni, Rosalba Del Coco, Elisabetta Mattioli, Daria Camozzi, Marta Columbaro, Elisa Schena, Luciano Merlini, Stefano Squarzoni, Nadir Mario Maraldi, Giovanna Lattanzi

Research output: Contribution to journalArticlepeer-review


Background information. Emerin is a nuclear envelope protein that contributes to nuclear architecture, chromatin structure, and gene expression through its interaction with various nuclear proteins. In particular, emerin is molecularly connected with the nuclear lamina, a protein meshwork composed of lamins and lamin-binding proteins underlying the inner nuclear membrane. Among nuclear lamina components, lamin A is a major emerin partner. Lamin A, encoded by the LMNA gene (lamin A/C gene), is produced as a precursor protein (prelamin A) that is post-transcriptionally modified at its C-terminal region where the CaaX motif triggers a sequence of modifications, including farnesylation, carboxymethylation, and proteolytic cleavage by ZMPSTE 24 (zinc metalloproteinase Ste24) metalloproteinase. Impairment of the lamin Amaturation pathway causing lamin A precursor accumulation is linked to the development of rare diseases such as familial partial lipodystrophy, MADA (mandibuloacral dysplasia), the Werner syndrome, Hutchinson-Gilford progeria syndrome and RD (restrictive dermopathy). Results. In the present study, we show that emerin and different prelamin A forms influence each other's localization. We show that the accumulation of non-farnesylated as well as farnesylated carboxymethylated lamin A precursors in human fibroblasts modifies emerin localization. On the contrary, emerin absence at the inner nuclear membrane leads to unprocessed (non-farnesylated) prelamin A aberrant localization only. Moreover, we observe that the restoration of emerin expression in emerin-null cells induces the recovery of non-farnesylated prelamin A localization. Conclusion. These results indicate that emerin-prelamin A interplay influences nuclear organization. This finding may be relevant to the understanding of laminopathies.

Original languageEnglish
Pages (from-to)541-554
Number of pages14
JournalBiology of the cell / under the auspices of the European Cell Biology Organization
Issue number9
Publication statusPublished - 2009


  • Emerin
  • Fibroblast
  • Laminopathy
  • Prelamin A
  • X-linked Emery-dreifuss muscular dystrophy type 1 (EDMD1)

ASJC Scopus subject areas

  • Cell Biology
  • Medicine(all)


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