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1.
Mol Biol Cell ; 21(15): 2707-20, 2010 Aug 01.
Article in English | MEDLINE | ID: mdl-20554764

ABSTRACT

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.


Subject(s)
Actins/metabolism , Caenorhabditis elegans Proteins/genetics , Caenorhabditis elegans/genetics , Cytoplasmic Dyneins/genetics , Cytoskeleton/metabolism , Mutation/genetics , Alleles , Animals , Caenorhabditis elegans/cytology , Caenorhabditis elegans/embryology , Caenorhabditis elegans/metabolism , Caenorhabditis elegans Proteins/metabolism , Cytoplasmic Dyneins/metabolism , Cytoskeleton/drug effects , Depsipeptides/pharmacology , Dyneins/metabolism , Embryo, Nonmammalian/cytology , Embryo, Nonmammalian/drug effects , Embryo, Nonmammalian/metabolism , Gene Knockdown Techniques , Genes, Helminth , Genes, Suppressor , Gonads/cytology , Gonads/drug effects , Gonads/metabolism , Microtubule-Associated Proteins/metabolism , Microtubules/drug effects , Microtubules/metabolism , Pachytene Stage/drug effects , Protein Transport/drug effects , RNA Interference/drug effects , Suppression, Genetic/drug effects
2.
PLoS One ; 4(3): e4722, 2009.
Article in English | MEDLINE | ID: mdl-19266099

ABSTRACT

Microvesicles are plasma membrane-derived vesicles released into the extracellular environment by a variety of cell types. Originally characterized from platelets, microvesicles are a normal constituent of human plasma, where they play an important role in maintaining hematostasis. Microvesicles have been shown to transfer proteins and RNA from cell to cell and they are also believed to play a role in intercellular communication. We characterized the RNA and protein content of embryonic stem cell microvesicles and show that they can be engineered to carry exogenously expressed mRNA and protein such as green fluorescent protein (GFP). We demonstrate that these engineered microvesicles dock and fuse with other embryonic stem cells, transferring their GFP. Additionally, we show that embryonic stem cells microvesicles contain abundant microRNA and that they can transfer a subset of microRNAs to mouse embryonic fibroblasts in vitro. Since microRNAs are short (21-24 nt), naturally occurring RNAs that regulate protein translation, our findings open up the intriguing possibility that stem cells can alter the expression of genes in neighboring cells by transferring microRNAs contained in microvesicles. Embryonic stem cell microvesicles may be useful therapeutic tools for transferring mRNA, microRNAs, protein, and siRNA to cells and may be important mediators of signaling within stem cell niches.


Subject(s)
Cell-Derived Microparticles/genetics , Embryonic Stem Cells/ultrastructure , MicroRNAs/metabolism , Animals , Biological Transport/genetics , Cell Communication/genetics , Cell-Derived Microparticles/metabolism , Embryonic Stem Cells/metabolism , Green Fluorescent Proteins , Mice , MicroRNAs/analysis
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