| First Author | Steiner-Champliaud MF | Year | 2010 |
| Journal | Exp Cell Res | Volume | 316 |
| Issue | 3 | Pages | 297-313 |
| PubMed ID | 19932097 | Mgi Jnum | J:156784 |
| Mgi Id | MGI:4421360 | Doi | 10.1016/j.yexcr.2009.11.010 |
| Citation | Steiner-Champliaud MF, et al. (2010) BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin. Exp Cell Res 316(3):297-313 |
| abstractText | BPAG1-b is the major muscle-specific isoform encoded by the dystonin gene, which expresses various protein isoforms belonging to the plakin protein family with complex, tissue-specific expression profiles. Recent observations in mice with either engineered or spontaneous mutations in the dystonin gene indicate that BPAG1-b serves as a cytolinker important for the establishment and maintenance of the cytoarchitecture and integrity of striated muscle. Here, we studied in detail its distribution in skeletal and cardiac muscles and assessed potential binding partners. BPAG1-b was detectable in vitro and in vivo as a high molecular mass protein in striated and heart muscle cells, co-localizing with the sarcomeric Z-disc protein alpha-actinin-2 and partially with the cytolinker plectin as well as with the intermediate filament protein desmin. Ultrastructurally, like alpha-actinin-2, BPAG1-b was predominantly localized at the Z-discs, adjacent to desmin-containing structures. BPAG1-b was able to form complexes with both plectin and alpha-actinin-2, and its NH(2)-terminus, which contains an actin-binding domain, directly interacted with that of plectin and alpha-actinin. Moreover, the protein level of BPAG1-b was reduced in muscle tissues from plectin-null mutant mice versus wild-type mice. These studies provide new insights into the role of BPAG1-b in the cytoskeletal organization of striated muscle. |
