http://www.cnr.it/ontology/cnr/individuo/prodotto/ID27405
Pre-Lamin A processing is linked to heterochromatin organization (Articolo in rivista)
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- Pre-Lamin A processing is linked to heterochromatin organization (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/jcb.21467 (literal)
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Lattanzi G, Columbaro M, Mattioli E, Cenni V, Camozzi D, Wehnert M, Santi S, Riccio M, Del Coco R, Maraldi NM, Squarzoni S, Foisner R, Capanni C. (2007)
Pre-Lamin A processing is linked to heterochromatin organization
in Journal of cellular biochemistry (Print)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lattanzi G, Columbaro M, Mattioli E, Cenni V, Camozzi D, Wehnert M, Santi S, Riccio M, Del Coco R, Maraldi NM, Squarzoni S, Foisner R, Capanni C. (literal)
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- IGM, CNR, Unit of Bologna, c/o IOR, Bologna, Italy; Laboratory of Cell Biology, Istituti Ortopedici Rizzoli, Bologna, Italy; Institute of Human Genetics, University of Greifswald, Germany; Department of Anatomy and Histology, University of Modena and Reggio Emilia, Modena, Italy; Max F. Perutz Laboratories, Medical University of Vienna, Vienna, Austria. (literal)
- Titolo
- Pre-Lamin A processing is linked to heterochromatin organization (literal)
- Abstract
- Pre-lamin A undergoes subsequent steps of post-translational modification at its C-terminus, including farnesylation, methylation, and cleavage by ZMPSTE24 metalloprotease. Here, we show that ccumulation of different intermediates of pre-lamin A processing in nuclei, induced by expression of mutated pre-lamin A, differentially affected chromatin organization in human fibroblasts. Unprocessed (non-farnesylated) pre-lamin A accumulated in intranuclear foci, caused the redistribution of LAP2alpha and of the heterochromatin markers HP1alpha and trimethyl-K9-histone 3, and triggered heterochromatin localization in the nuclear interior. In contrast, the farnesylated and carboxymethylated lamin A precursor accumulated at the nuclear periphery and caused loss of heterochromatin markers and Lap2alpha in enlarged nuclei. Interestingly, pre-lamin A bound both HP1alpha and LAP2alpha in vivo, but the farnesylated form showed reduced affinity for HP1alpha. Our data show a link between pre-lamin A processing and heterochromatin remodeling and have major implications for understanding molecular mechanisms of human diseases linked to mutations in lamins. (literal)
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