Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts

Giovanna Lattanzi, Vittoria Cenni, Sandra Marmiroli, Cristina Capanni, Elisabetta Mattioli, Luciano Merlini, Stefano Squarzoni, Nadir Mario Maraldi

Research output: Contribution to journalArticlepeer-review


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 α and β 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.

Original languageEnglish
Pages (from-to)764-770
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - Apr 11 2003


  • Actin
  • Emerin
  • Myoblast differentiation
  • Protein phosphatase 1
  • Protein-protein interaction
  • Serine-threonine phosphatase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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