Prelamin A is involved in early steps of muscle differentiation

Cristina Capanni, Rosalba Del Coco, Stefano Squarzoni, Marta Columbaro, Elisabetta Mattioli, Daria Camozzi, Anna Rocchi, Katia Scotlandi, Nadir Maraldi, Roland Foisner, Giovanna Lattanzi

Research output: Contribution to journalArticlepeer-review


Lamin A is a nuclear lamina constituent implicated in a number of human disorders including Emery-Dreifuss muscular dystrophy. Since increasing evidence suggests a role of the lamin A precursor in nuclear functions, we investigated the processing of prelamin A during differentiation of C2C12 mouse myoblasts. We show that both protein levels and cellular localization of prelamin A are modulated during myoblast activation. Similar changes of lamin A-binding proteins emerin and LAP2α were observed. Furthermore, prelamin A was found in a complex with LAP2α in differentiating myoblasts. Prelamin A accumulation in cycling myoblasts by expressing unprocessable mutants affected LAP2α and PCNA amount and increased caveolin 3 mRNA and protein levels, while accumulation of prelamin A in differentiated muscle cells following treatment with a farnesyl transferase inhibitor appeared to inhibit caveolin 3 expression. Our data provide evidence for a critical role of the lamin A precursor in the early steps of muscle cell differentiation.

Original languageEnglish
Pages (from-to)3628-3637
Number of pages10
JournalExperimental Cell Research
Issue number20
Publication statusPublished - Dec 10 2008


  • Caveolin 3
  • LAP2 alpha
  • Myoblast differentiation
  • Prelamin A

ASJC Scopus subject areas

  • Cell Biology


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