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Literature DB >> 19584095

Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum.

Stephan Lange¹, Kunfu Ouyang, Gretchen Meyer, Li Cui, Hongqiang Cheng, Richard L Lieber, Ju Chen.

Abstract

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.

Entities: Disease Gene Species

Mesh：

Substances：

Year: 2009 PMID： 19584095 PMCID： PMC2909316 DOI： 10.1242/jcs.046193

Source DB: PubMed Journal: J Cell Sci ISSN： 0021-9533 Impact factor: 5.285

51 in total

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9. Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy.

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10. Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly.

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7. Exercise-induced alterations and loss of sarcomeric M-line organization in the diaphragm muscle of obscurin knockout mice.

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