Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum | Zendy

Stephan Lange | Zendy; Kunfu Ouyang | Zendy; Gretchen A. Meyer | Zendy; Li Cui | Zendy; Hongqiang Cheng | Zendy; Richard L. Lieber | Zendy; Ju Chen | Zendy

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Obscurin determines the architecture of the longitudinal sarcoplasmic reticulum

Author(s) -

Stephan Lange,

Kunfu Ouyang,

Gretchen A. Meyer,

Li Cui,

Hongqiang Cheng,

Richard L. Lieber,

Ju Chen

Publication year - 2009

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.046193

Subject(s) - obscurin , titin , sarcomere , biology , ankyrin , endoplasmic reticulum , microbiology and biotechnology , ankyrin repeat , skeletal muscle , myocyte , myofilament , spectrin , cytoskeleton , cell , genetics , anatomy , gene

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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