http://www.cnr.it/ontology/cnr/individuo/prodotto/ID27617

Emerin-prelamin A interplay in human fibroblasts. (Articolo in rivista)

Type

Articolo in rivista (Classe)
Prodotto della ricerca (Classe)

Label

Emerin-prelamin A interplay in human fibroblasts. (Articolo in rivista) (literal)

Anno

2009-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1042/BC20080175 (literal)

Alternative label

Capanni C, Del Coco R, Mattioli E, Camozzi D, Columbaro M, Schena E, Merlini L, Squarzoni S, Maraldi NM, Lattanzi G. (2009)
Emerin-prelamin A interplay in human fibroblasts.
in Biology of the cell (Online)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Capanni C, Del Coco R, Mattioli E, Camozzi D, Columbaro M, Schena E, Merlini L, Squarzoni S, Maraldi NM, Lattanzi G. (literal)

Pagina inizio

541 (literal)

Pagina fine

554 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

101 (literal)

Rivista

Biology of the cell (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

16 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

9 (literal)

Note

ISI Web of Science (WOS) (literal)
Pubme (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

IGM-CNR, Unit of Bologna c/o IOR, Via di Barbiano 1/10, Bologna, 40136, Italy; Laboratory of Cell Biology and Electron Microscopy, IOR, Via di Barbiano 1/10, Bologna, 40136, Italy; Department of Experimental and Diagnostic Medicine, Section of Medical Genetics, University of Ferrara, Via Fossato di Mortara, Ferrara, 44100, Italy (literal)

Titolo

Emerin-prelamin A interplay in human fibroblasts. (literal)

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. (literal)

Prodotto di