Abstract
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 language | English |
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Pages (from-to) | 3628-3637 |
Number of pages | 10 |
Journal | Experimental Cell Research |
Volume | 314 |
Issue number | 20 |
DOIs | |
Publication status | Published - Dec 10 2008 |
Keywords
- Caveolin 3
- LAP2 alpha
- Myoblast differentiation
- Prelamin A
ASJC Scopus subject areas
- Cell Biology