Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

104 Scopus citations


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 β-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.

Original languageEnglish (US)
Pages (from-to)2640-2650
Number of pages11
JournalJournal of cell science
Issue number15
StatePublished - Aug 1 2009


  • Ankyrin
  • Knockout
  • Muscular dystrophy
  • Nedd8
  • Obscurin
  • Sarcoplasmic reticulum

ASJC Scopus subject areas

  • Cell Biology


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