| First Author | Lange S | Year | 2009 |
| Journal | J Cell Sci | Volume | 122 |
| Issue | Pt 15 | Pages | 2640-50 |
| PubMed ID | 19584095 | Mgi Jnum | J:153150 |
| Mgi Id | MGI:4361072 | Doi | 10.1242/jcs.046193 |
| Citation | Lange S, et al. (2009) Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum. J Cell Sci 122(Pt 15):2640-50 |
| abstractText | The giant protein obscurin is thought to link the sarcomere with the sarcoplasmic reticulum (SR). The N-terminus of obscurin interacts with the M-band proteins titin and myomesin, whereas the C-terminus mediates interactions with ankyrin proteins. Here, we investigate the importance of obscurin for SR architecture and organization. Lack of obscurin in cross-striated muscles leads to changes in longitudinal SR architecture and disruption of small ankyrin-1.5 (sAnk1.5) expression and localization. Changes in SR architecture in obscurin knockout mice are also associated with alterations in several SR or SR-associated proteins, such as ankyrin-2 and beta-spectrin. Finally, obscurin knockout mice display centralized nuclei in skeletal muscles as a sign of mild myopathy, but have normal sarcomeric structure and preserved muscle function. |
