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Resources » Paper

Spooner, Patrick et al. (2011) International Worm Meeting "Immunoglobulin domain containing isoforms of UNC-89 (obscurin) are required for myofilament organization and calcium signaling in Caenorhabditis elegans."

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00038601

    Spooner, Patrick, Duran, M. Berenice, Bonner, Jennifer, Benian, Guy, & Norman, Kenneth (2011). Immunoglobulin domain containing isoforms of UNC-89 (obscurin) are required for myofilament organization and calcium signaling in Caenorhabditis elegans presented in International Worm Meeting. Unpublished information; cite only with author permission.

    The force generating machinery in muscle is regulated by the influx of calcium ions into the muscle cytoplasm. Initially, depolarization of the sarcolemma leads to calcium entry via voltage gated calcium channels, which rapidly triggers the release of calcium from the sarcoplasmic reticulum via ryanodine receptors by calcium induced calcium release. Thus, calcium needs to be rapidly, accurately and reliably regulated and the calcium channels and contractile machinery must be maintained in a highly ordered arrangement for efficient and effective muscle contraction to occur. The mechanism underlying this highly organized configuration is not fully understood. Using a combination of genetic and cell biological techniques, we have found that the C. elegans ortholog of the giant muscle protein obscurin, UNC-89, is required for muscle cell organization. The unc-89 locus encodes at least 6 isoforms as large as 900 kDa, 4 large Immunoglobin (Ig) domain rich isoforms and two smaller tandem kinase containing isoforms (Small et al. 2004; Ferrara et al. 2005). From our analyses, we have found that large Ig domain rich isoforms of UNC-89 are critical for sarcomere and SR organization. Furthermore, we have found evidence that unc-89 mutants lacking the large Ig rich isoforms have defects in excitation-contraction coupling in the pharyngeal and body wall muscle, through the coordination of calcium influx. Thus, our data implicates the large Ig domain rich isoforms of UNC-89 in maintaining muscle cell architecture that is critical for efficient and effective muscle contraction.

    Affiliations:
    - Department of Biology, Skidmore College, Saratoga Springs, NY
    - Department of Pathology, Emory University, Atlanta, GA
    - Center for Cell Biology & Cancer Research, Albany Medical College, Albany, NY.


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