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J Cell Sci. 2009 Aug 1;122(Pt 15):2640-50. doi: 10.1242/jcs.046193. Epub 2009 Jul 7.

Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum.

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Department of Medicine, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.


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.

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