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Cytoplasmic dynein light intermediate ch ... tosis in Caenorhabditis elegans
Cytoplasmic dynein light intermediate chain is required for discrete aspects of mitosis in Caenorhabditis elegans.
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We describe phenotypic characterization of dli-1, the Caenorhabditis elegans homolog of cytoplasmic dynein light intermediate chain (LIC), a subunit of the cytoplasmic dynein motor complex. Animals homozygous for loss-of-function mutations in dli-1 exhibit stochastic failed divisions in late larval cell lineages, resulting in zygotic sterility. dli-1 is required for dynein function during mitosis. Depletion of the dli-1 gene product through RNA-mediated gene interference (RNAi) reveals an early embryonic requirement. One-cell dli-1(RNAi) embryos exhibit failed cell division attempts, resulting from a variety of mitotic defects. Specifically, pronuclear migration, centrosome separation, and centrosome association with the male pronuclear envelope are defective in dli-1(RNAi) embryos. Meiotic spindle formation, however, is not affected in these embryos. DLI-1, like its vertebrate homologs, contains a putative nucleotide-binding domain similar to those found in the ATP-binding cassette transporter family of ATPases as well as other nucleotide-binding and -hydrolyzing proteins. Amino acid substitutions in a conserved lysine residue, known to be required for nucleotide binding, confers complete rescue in a dli-1 mutant background, indicating this is not an essential domain for DLI-1 function.
Yoder JH, Han M
Molecular biology of the cell
2001-10-01 00:00
12
10
2921-33
Alleles,Animals,Caenorhabditis elegans,Caenorhabditis elegans Proteins,Centrosome,Cloning, Molecular,Cytoplasm,Dynein ATPase,Meiosis,Mitosis,Mitotic Spindle Apparatus,Molecular Sequence Data,Nuclear Envelope,Phenotype,Point Mutation,Protein Structure, Tertiary,Protein Subunits,Sequence Alignment,Caenorhabditis elegans Proteins,Protein Subunits,Dli-1 protein, C elegans,Dynein ATPase
Department of Molecular, Cellular, and Developmental Biology, Howard Hughes Medical Institution, University of Colorado, Boulder, 80303-0347, USA
Mol. Biol. Cell
NIGMS GM-47869
1059-1524
478
True
11598181
