Prelamin A is involved in early steps of muscle differentiation
- IGM-CNR, Unit of Bologna, c/o IOR, Via di Barbiano 1/10 I-40136 Bologna (Italy)
- Laboratory of Cell Biology Istituto Ortopedico Rizzoli, Bologna (Italy)
- Laboratory of Oncological Research, Istituto Ortopedico Rizzoli, Bologna (Italy)
- Max F. Perutz Laboratories, Medical University of Vienna, Vienna (Austria)
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 LAP2{alpha} were observed. Furthermore, prelamin A was found in a complex with LAP2{alpha} in differentiating myoblasts. Prelamin A accumulation in cycling myoblasts by expressing unprocessable mutants affected LAP2{alpha} 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.
- OSTI ID:
- 21176147
- Journal Information:
- Experimental Cell Research, Vol. 314, Issue 20; Other Information: DOI: 10.1016/j.yexcr.2008.09.026; PII: S0014-4827(08)00388-1; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0014-4827
- Country of Publication:
- United States
- Language:
- English
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