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Emerin-prelamin A interplay in human fibroblasts
- Source :
- Biology of the Cell. 101:541-554
- Publication Year :
- 2009
- Publisher :
- Wiley, 2009.
-
Abstract
- 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 A maturation 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.
- Subjects :
- congenital, hereditary, and neonatal diseases and abnormalities
Emerin
Laminopathy
Biology
Cell Line
LMNA
medicine
Humans
Inner membrane
Protein Precursors
Nuclear protein
Cells, Cultured
Progeria
integumentary system
Membrane Proteins
Nuclear Proteins
nutritional and metabolic diseases
Cell Biology
General Medicine
Fibroblasts
Lamin Type A
medicine.disease
Cell biology
Protein Transport
Biochemistry
embryonic structures
Nuclear lamina
Protein Processing, Post-Translational
Lamin
Protein Binding
Subjects
Details
- ISSN :
- 02484900
- Volume :
- 101
- Database :
- OpenAIRE
- Journal :
- Biology of the Cell
- Accession number :
- edsair.doi.dedup.....f4f2f78bee24a640a5e9f376f6410a5e