Abstract
Mutations in anc-1 (nuclear anchorage defective) disrupt the positioning of nuclei and mitochondria in Caenorhabditis elegans. ANC-1 is shown to consist of mostly coiled regions with a nuclear envelope localization domain (called the KASH domain) and an actin-binding domain; this structure was conserved with the Drosophila protein Msp-300 and the mammalian Syne proteins. Antibodies against ANC-1 localized cytoplasmically and were enriched at the nuclear periphery in an UNC-84-dependent manner. Overexpression of the KASH domain or the actin-binding domain caused a dominant negative anchorage defect. Thus, ANC-1 may connect nuclei to the cytoskeleton by interacting with UNC-84 at the nuclear envelope and with actin in the cytoplasm.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / metabolism*
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Alleles
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Animals
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Animals, Genetically Modified
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Caenorhabditis elegans / genetics
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Caenorhabditis elegans / metabolism*
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Caenorhabditis elegans / ultrastructure
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Caenorhabditis elegans Proteins / analysis
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Caenorhabditis elegans Proteins / chemistry
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Caenorhabditis elegans Proteins / genetics
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Caenorhabditis elegans Proteins / metabolism*
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Cell Nucleus / metabolism*
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Cytoplasm / chemistry
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Cytoskeleton / metabolism*
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Genes, Helminth
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Membrane Glycoproteins / metabolism
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Microfilament Proteins / analysis
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Mitochondria / ultrastructure
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Mutation
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Nuclear Envelope / chemistry
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Nuclear Envelope / genetics
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Nuclear Envelope / metabolism
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Nuclear Proteins / metabolism
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Phenotype
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / metabolism
Substances
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ANC-1 protein, C elegans
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Actins
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Caenorhabditis elegans Proteins
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Membrane Glycoproteins
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Microfilament Proteins
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Nuclear Proteins
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Recombinant Fusion Proteins
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Unc-84 protein, C elegans