Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. (Articolo in rivista)

Type

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

Label

• Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (2003)
  Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts.
  in Biochemical and biophysical research communications (Print)
  (literal)

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

• Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (literal)

Pagina inizio

• 764 (literal)

Pagina fine

• 770 (literal)

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

• 303 (literal)

Rivista

• Biochemical and biophysical research communications (Rivista)

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

• I.F. 2,935 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• ITOI-CNR, Unit of Bologna, c/o IOR, Via di Barbiano, 1/10, I-40136 Bologna, Italy (literal)

Titolo

• Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. (literal)

Abstract

• Emerin is a nuclear envelope protein whose biological function remains to be elucidated. Mutations of emerin gene cause the Emery-Dreifuss muscular dystrophy, a neuromuscular disorder also linked to mutations of lamin A/C. In this paper, we analyze the interaction between emerin and actin in differentiating mouse myoblasts. We demonstrate that emerin and lamin A/C are bound to actin at the late stages of myotube differentiation and in mature muscle. The interaction involves both nuclear alpha and beta actins and cytoplasmic actin. A serine-threonine phosphatase activity markedly increases emerin-actin binding even in cycling myoblasts. This effect is also observed with purified nuclear fractions in pull-down assay. On the other hand, active protein phosphatase 1, a serine-threonine phosphatase known to associate with lamin A/C, inhibits emerin-actin interaction in myotube extracts. These data provide evidence of a modulation of emerin-actin interaction in muscle cells, possibly through differentiation-related stimuli. (literal)

Autore CNR

• STEFANO SQUARZONI (Persona)
• CRISTINA CAPANNI (Persona)
• VITTORIA CENNI (Unità di personale interno)
• GIOVANNA LATTANZI (Persona)

Incoming links:

Autore CNR di

• GIOVANNA LATTANZI (Persona)
• STEFANO SQUARZONI (Persona)
• CRISTINA CAPANNI (Persona)
• VITTORIA CENNI (Unità di personale interno)

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

• Biochemical and biophysical research communications (Rivista)