| First Author | Lattanzi G | Year | 2003 |
| Journal | Biochem Biophys Res Commun | Volume | 303 |
| Issue | 3 | Pages | 764-70 |
| PubMed ID | 12670476 | Mgi Jnum | J:83147 |
| Mgi Id | MGI:2657074 | Doi | 10.1016/s0006-291x(03)00415-7 |
| Citation | Lattanzi G, et al. (2003) Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. Biochem Biophys Res Commun 303(3):764-70 |
| abstractText | 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. |
