| First Author | Depreux FF | Year | 2015 |
| Journal | Hum Mol Genet | Volume | 24 |
| Issue | 15 | Pages | 4284-95 |
| PubMed ID | 25948554 | Mgi Jnum | J:224003 |
| Mgi Id | MGI:5661090 | Doi | 10.1093/hmg/ddv160 |
| Citation | Depreux FF, et al. (2015) Disruption of the lamin A and matrin-3 interaction by myopathic LMNA mutations. Hum Mol Genet 24(15):4284-95 |
| abstractText | The nuclear face of the nuclear membrane is enriched with the intermediate filament protein lamin A. Mutations in LMNA, the gene encoding lamin A, lead to a diverse set of inherited conditions including myopathies that affect both the heart and skeletal muscle. To gain insight about lamin A protein interactions, binding proteins associated with the tail of lamin A were characterized. Of 130 nuclear proteins found associated with the lamin A tail, 17 (13%) were previously described lamin A binding partners. One protein not previously linked to lamin A, matrin-3, was selected for further study, because like LMNA mutations, matrin-3 has also been implicated in inherited myopathy. Matrin-3 binds RNA and DNA and is a nucleoplasmic protein originally identified from the insoluble nuclear fraction, referred to as the nuclear matrix. Anti-matrin-3 antibodies were found to co-immunoprecipitate lamin A, and the lamin-A binding domain was mapped to the carboxy-terminal half of matrin-3. Three-dimensional mapping of the lamin A-matrin-3 interface showed that the LMNA truncating mutation Delta303, which lacks the matrin-3 binding domain, was associated with an increased distance between lamin A and matrin-3. LMNA mutant cells are known to have altered biophysical properties and the matrin-3-lamin A interface is positioned to contribute to these defects. |
