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Resources » Paper

Miller RK et al. (2008) Mol Biol Cell "UNC-98 and UNC-96 interact with paramyosin to promote its incorporation into thick filaments of Caenorhabditis elegans."

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  • Comments on Miller RK et al. (2008) Mol Biol Cell "UNC-98 and UNC-96 interact with paramyosin to promote its incorporation into thick filaments of Caenorhabditis elegans." (0)

  • Overview

    PMID:
    18256289
    DOI:
    10.1091/mbc.E07-07-0723
    Status:
    Publication type:
    Journal_article
    WormBase ID:
    WBPaper00031500

    Miller RK, Qadota H, Mercer KB, Gernert KM, & Benian GM (2008). UNC-98 and UNC-96 interact with paramyosin to promote its incorporation into thick filaments of Caenorhabditis elegans. Mol Biol Cell, 19, 1529-39. doi:10.1091/mbc.E07-07-0723

    Monitoring Editor: Thomas Pollard Mutations in unc-96 or unc-98 cause reduced motility and a characteristic defect in muscle structure: by polarized light microscopy birefringent needles are found at the ends of muscle cells. Anti-paramyosin stains the needles in unc-96 and unc-98 mutant muscle. However there is no difference in the overall level of paramyosin in wild-type, unc-96 and unc-98 animals. Anti-UNC-98 and anti-paramyosin colocalize in the paramyosin accumulations of missense alleles of unc-15 (encodes paramyosin). Anti-UNC-96 (Mercer et al., 2006) and anti-UNC-98 have diffuse localization within muscles of unc-15 null mutants. By immunoblot, in the absence of paramyosin, UNC-98 is diminished, whereas in paramysoin missense mutants, UNC-98 is increased. unc-98 and unc-15, or unc-96 and unc-15 (Mercer et al., 2006) interact genetically either as double heterozygotes or as double homozygotes. By yeast 2-hybrid and ELISAs using purified proteins, UNC-98 interacts with paramyosin residues 31-693, whereas UNC-96 interacts with a separate region of paramyosin, residues 699-798. The importance of surface charge of this 99 residue region for UNC-96 binding was shown. Paramyosin lacking the C terminal UNC-96 binding region fails to localize throughout A-bands. We propose a model in which UNC-98 and UNC-96 may act as chaperones to promote the incorporation of paramyosin into thick filaments.


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