ArticleMolecular biology of the cell2009
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.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 40 citations in OpenAlex.
- The myosin chaperone UNC-45 has an important role in maintaining the structure and function of muscle sarcomeres during adult aging.Molecular biology of the cell · 2024Article
- Article
- COP9 signalosome component CSN-5 stabilizes PUF proteins FBF-1 and FBF-2 in Caenorhabditis elegans germline stem and progenitor cells.Genetics · 2024Article
- The RhoGAP RRC-1 is required for the assembly or stability of integrin adhesion complexes and is a member of the PIX pathway in muscle.Molecular biology of the cell · 2024Article
- Transcriptome-wide association study identifies novel genes associated with bone mineral density and lean body mass in children.Endocrine · 2023Article
- Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity.Protein science : a publication of the Protein Society · 2021Article
- Effects of targeting sumoylation processes during latent and induced Epstein-Barr virus infections using the small molecule inhibitor ML-792.Antiviral research · 2021Article
- The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease.International journal of molecular sciences · 2020Review
- The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020Review
- The Role of the UNC-82 Protein Kinase in Organizing Myosin Filaments in Striated Muscle ofGenetics · 2017Article
- The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle.Molecular biology of the cell · 2016Article
- The CSN/COP9 signalosome regulates synaptonemal complex assembly during meiotic prophase I of Caenorhabditis elegans.PLoS genetics · 2014Article
- Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction.Biopolymers · 2014Article
- Membrane-myofibril cross-talk in myofibrillogenesis and in muscular dystrophy pathogenesis: lessons from the zebrafish.Frontiers in physiology · 2014Article
- A novel platform for virus-like particle-display of flaviviral envelope domain III: induction of Dengue and West Nile virus neutralizing antibodies.Virology journal · 2013Article
- Breaking down protein degradation mechanisms in cardiac muscle.Trends in molecular medicine · 2013Review
- Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover.Molecular biology of the cell · 2012Article
- UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans.Molecular biology of the cell · 2012Article
- Bending amplitude - a new quantitative assay of C. elegans locomotion: identification of phenotypes for mutants in genes encoding muscle focal adhesion components.Methods (San Diego, Calif.) · 2012Article
- Immunofluorescent localization of proteins in Caenorhabditis elegans muscle.Methods in molecular biology (Clifton, N.J.) · 2012Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
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.
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