Staurosporine treatment and serum starvation promote the cleavage of emerin in cultured mouse myoblasts: Involvement of a caspase-dependent mechanism

Marta Columbaro, Elisabetta Mattioli, Giovanna Lattanzi, Cristina Rutigliano, Andrea Ognibene, Nadir Mario Maraldi, Stefano Squarzoni

Research output: Contribution to journalArticle

Abstract

Emerin is a nuclear membrane-anchored protein which is absent or mutated in patients affected by Emery-Dreifuss muscular dystrophy. In this study, we induced apoptosis in cultured mouse myoblasts to evaluate emerin fate during the nuclear destabilization involved in programmed cell death. Emerin proteolysis was observed in myocytes during the apoptotic process. Myoblast apoptosis and emerin degradation were associated with chromatin compaction and detachment from the nuclear lamina, as detected by electron microscopy. In vivo specific inhibition of caspase 3 or caspase 6 activity completely abolished emerin proteolysis. These results show that the process of programmed cell death in muscle cells leads to emerin proteolysis, which appears to be related to caspase 6 activation and to cleavage of other nuclear envelope proteins, that share sequence homologies or functional features with emerin.

Original languageEnglish
Pages (from-to)423-429
Number of pages7
JournalFEBS Letters
Volume509
Issue number3
DOIs
Publication statusPublished - Dec 14 2001

Keywords

  • Apoptosis
  • Caspase 3
  • Caspase 6
  • Emerin
  • Myoblast
  • Nuclear envelope

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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