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MBC in Press, published online ahead of print June 17, 2009
Mol. Biol. Cell 10.1091/mbc.E09-03-0208

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Submitted on March 13, 2009
Revised on June 4, 2009
Accepted on June 5, 2009

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

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

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

Monitoring Editor: William P. Tansey

In C. 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 UNC-96 using the yeast 2-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 UNC-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, unc-96, and unc-15 (encodes paramyosin) mutants. Double knock down of csn-5 and csn-6 could slightly suppress the unc-96 mutant phenotype. In the double knock down of csn-5 and csn-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 UNC-96, two M-line proteins.

{sect}these authors contributed equally to this work.

Present addresses: {ddagger}Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030; ||Division of Biological Sciences, University of California, San Diego, La Jolla, California 92093; Department of Human Genetics, Emory University, Atlanta, Georgia, 30322.

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






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