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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2010-7-30
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pubmed:abstractText |
Functional analysis of cytoplasmic dynein in Caenorhabditis elegans has revealed a wide range of cellular functions for this minus-end-directed motor protein. Dynein transports a variety of cargos to diverse cellular locations, and thus cargo selection and destination are likely regulated by accessory proteins. The microtubule-associated proteins LIS-1 and dynein interact, but the nature of this interaction remains poorly understood. Here we show that both LIS-1 and the dynein heavy-chain DHC-1 are required for integrity of the actin cytoskeleton in C. elegans. Although both dhc-1(or195ts) and lis-1 loss-of-function disrupt the actin cytoskeleton and produce embryonic lethality, a double mutant suppresses these defects. A targeted RNA interference screen revealed that knockdown of other actin regulators, including actin-capping protein genes and prefoldin subunit genes, suppresses dhc-1(or195ts)-induced lethality. We propose that release or relocation of the mutant dynein complex mediates this suppression of dhc-1(or195ts)-induced phenotypes. These results reveal an unexpected direct or indirect interaction between the actin cytoskeleton and dynein activity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoplasmic Dyneins,
http://linkedlifedata.com/resource/pubmed/chemical/DHC-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Depsipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Dyneins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/jasplakinolide,
http://linkedlifedata.com/resource/pubmed/chemical/lis-1 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1939-4586
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2707-20
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pubmed:meshHeading |
pubmed-meshheading:20554764-Actins,
pubmed-meshheading:20554764-Alleles,
pubmed-meshheading:20554764-Animals,
pubmed-meshheading:20554764-Caenorhabditis elegans,
pubmed-meshheading:20554764-Caenorhabditis elegans Proteins,
pubmed-meshheading:20554764-Cytoplasmic Dyneins,
pubmed-meshheading:20554764-Cytoskeleton,
pubmed-meshheading:20554764-Depsipeptides,
pubmed-meshheading:20554764-Dyneins,
pubmed-meshheading:20554764-Embryo, Nonmammalian,
pubmed-meshheading:20554764-Gene Knockdown Techniques,
pubmed-meshheading:20554764-Genes, Helminth,
pubmed-meshheading:20554764-Genes, Suppressor,
pubmed-meshheading:20554764-Gonads,
pubmed-meshheading:20554764-Microtubule-Associated Proteins,
pubmed-meshheading:20554764-Microtubules,
pubmed-meshheading:20554764-Mutation,
pubmed-meshheading:20554764-Pachytene Stage,
pubmed-meshheading:20554764-Protein Transport,
pubmed-meshheading:20554764-RNA Interference,
pubmed-meshheading:20554764-Suppression, Genetic
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pubmed:year |
2010
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pubmed:articleTitle |
Regulators of the actin cytoskeleton mediate lethality in a Caenorhabditis elegans dhc-1 mutant.
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pubmed:affiliation |
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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