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Vol. 20, Issue 15, 3608-3616, August 1, 2009

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CSN-5, a Component of the COP9 Signalosome Complex, Regulates the Levels of UNC-96 and UNC-98, Two Components of M-lines in Caenorhabditis elegans Muscle

Rachel K. Miller^*,,,, Hiroshi Qadota^*,, Thomas J. Stark^*,||, Kristina B. Mercer^*,¶, Tesheka S. Wortham^*,, Akwasi Anyanful^*, and Guy M. Benian^*

*Department of Pathology and Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322

Submitted March 13, 2009; Revised June 4, 2009; Accepted June 5, 2009
Monitoring Editor: William P. Tansey

In Caenorhabditis elegans two M-line proteins, UNC-98 and UNC-96, are involved in myofibril assembly and/or maintenance, especially myosin thick filaments. We found that CSN-5, a component of the COP9 signalosome complex, binds to UNC-98 and -96 using the yeast two-hybrid method. These interactions were confirmed by biochemical methods. The CSN-5 protein contains a Mov34 domain. Although one other COP9 signalosome component, CSN-6, also has a Mov34 domain, CSN-6 did not interact with UNC-98 or -96. Anti-CSN-5 antibody colocalized with paramyosin at A-bands in wild type and colocalized with abnormal accumulations of paramyosin found in unc-98, -96, and -15 (encodes paramyosin) mutants. Double knockdown of csn-5 and -6 could slightly suppress the unc-96 mutant phenotype. In the double knockdown of csn-5 and -6, the levels of UNC-98 protein were increased and the levels of UNC-96 protein levels were slightly reduced, suggesting that CSN-5 promotes the degradation of UNC-98 and that CSN-5 stabilizes UNC-96. In unc-15 and unc-96 mutants, CSN-5 protein was reduced, implying the existence of feed back regulation from myofibril proteins to CSN-5 protein levels. Taken together, we found that CSN-5 functions in muscle cells to regulate UNC-98 and -96, two M-line proteins.

These authors contributed equally to this work.

Present addresses: Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, TX 77030;

^||Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093;

^¶Department of Human Genetics, Emory University, Atlanta, GA 30322.

Address correspondence to: Guy M. Benian (pathgb{at}emory.edu)

Abbreviations used: ECL, enhanced chemiluminescence; HA, hemagglutinin; MBP, maltose-binding protein.

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