Linked Life Data

20554764

Source:http://linkedlifedata.com/resource/pubmed/id/20554764

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pubmed-article:20554764pubmed:dateCreated2010-7-30lld:pubmed
pubmed-article:20554764pubmed:abstractTextFunctional 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.lld:pubmed
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pubmed-article:20554764pubmed:year2010lld:pubmed
pubmed-article:20554764pubmed:articleTitleRegulators of the actin cytoskeleton mediate lethality in a Caenorhabditis elegans dhc-1 mutant.lld:pubmed
pubmed-article:20554764pubmed:affiliationDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.lld:pubmed
pubmed-article:20554764pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:20554764pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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