Characterization of a Novel Dp71 Dystrophin-associated Protein Complex (Dapc) Present in the Nucleus of Hela Cells: Members of the Nuclear Dapc Associate with the Nuclear Matrix.
From: Department of Genetics and Molecular Biology, Centro de Investigación y de Estudios Avanzados del IPN, Avenida Instituto Politécnico Nacional 2508, Apartado Postal 14-740, C.P. 07000, México D.F., México.
Experimental cell research
- Publish Date: Oct 2006
- ISSN: 0014-4827
- Volume: 312
- Issue: 16
- Pages: 3023-35
- Medium: Print
- Language: English
- Citation (JAMA): Fuentes-Mera Lizeth, Rodríguez-Muñoz Rafael, González-Ramírez Ricardo, et al. Characterization of a Novel Dp71 Dystrophin-associated Protein Complex (Dapc) Present in the Nucleus of Hela Cells: Members of the Nuclear Dapc Associate with the Nuclear Matrix.. Exp. Cell Res. Oct 2006;312:3023-35
Abstract
Dystrophin is an essential component in the assembly and maintenance of the dystrophin-associated protein complex (DAPC), which includes members of the dystroglycan, syntrophin, sarcoglycan and dystrobrevin protein families. Distinctive complexes have been described in the cell membrane of different tissues and cultured cells. In this work, we report the identification and characterization of a novel DAPC present in the nuclei of HeLa cells, which contains dystrophin Dp71 as a key component. Using confocal microscopy and cell fractionation analyses, we found the presence of Dp71, beta-sarcoglycan, beta-dystroglycan, alpha- and beta-syntrophin, alpha1- and beta-dystrobrevin and nNOS in the nuclei of HeLa cells. Furthermore, we demonstrated by co-immunoprecipitation experiments that most of these proteins form a complex in the nuclear compartment. Next, we analyze the possible association of the nuclear DAPC with the nuclear matrix. We found the presence of Dp71, beta-dystroglycan, nNOS, beta-sarcoglycan, alpha/beta syntrophin, alpha1-dystrobrevin and beta-dystrobrevin in the nuclear matrix protein fractions and in situ nuclear matrix preparations from HeLa cells. Moreover, we found that Dp71, beta-dystroglycan and beta-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. The association of members of the nuclear DAPC with the nuclear matrix indicates that they may work as scaffolding proteins involved in nuclear architecture.
Mesh Headings (Keywords): Actins, Cells, Cultured, Dystrophin, Dystrophin-Associated Protein Complex, Hela Cells, Humans, Lamin Type B, Nuclear Matrix, Protein Binding, Protein Isoforms, Protein Transport, Subcellular Fractions
Check for Full Text / PubMed Unique Identifier (PMID): 16824516
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