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1.
PLoS Genet ; 4(3): e1000043, 2008 Mar 28.
Article in English | MEDLINE | ID: mdl-18369461

ABSTRACT

Migration of cells within epithelial sheets is an important feature of embryogenesis and other biological processes. Previous work has demonstrated a role for inositol 1,4,5-trisphosphate (IP(3))-mediated calcium signalling in the rearrangement of epidermal cells (also known as hypodermal cells) during embryonic morphogenesis in Caenorhabditis elegans. However the mechanism by which IP(3) production is stimulated is unknown. IP(3) is produced by the action of phospholipase C (PLC). We therefore surveyed the PLC family of C. elegans using RNAi and mutant strains, and found that depletion of PLC-1/PLC-epsilon produced substantial embryonic lethality. We used the epithelial cell marker ajm-1::gfp to follow the behaviour of epidermal cells and found that 96% of the arrested embryos have morphogenetic defects. These defects include defective ventral enclosure and aberrant dorsal intercalation. Using time-lapse confocal microscopy we show that the migration of the ventral epidermal cells, especially of the leading cells, is slower and often fails in plc-1(tm753) embryos. As a consequence plc-1 loss of function results in ruptured embryos with a Gex phenotype (gut on exterior) and lumpy larvae. Thus PLC-1 is involved in the regulation of morphogenesis. Genetic studies using gain- and loss-of-function alleles of itr-1, the gene encoding the IP(3) receptor in C. elegans, demonstrate that PLC-1 acts through ITR-1. Using RNAi and double mutants to deplete the other PLCs in a plc-1 background, we show that PLC-3/PLC-gamma and EGL-8/PLC-beta can compensate for reduced PLC-1 activity. Our work places PLC-epsilon into a pathway controlling epidermal cell migration, thus establishing a novel role for PLC-epsilon.


Subject(s)
Caenorhabditis elegans Proteins/physiology , Caenorhabditis elegans/embryology , Caenorhabditis elegans/enzymology , Phosphoinositide Phospholipase C/physiology , Animals , Animals, Genetically Modified , Base Sequence , Caenorhabditis elegans/genetics , Caenorhabditis elegans Proteins/antagonists & inhibitors , Caenorhabditis elegans Proteins/genetics , DNA Primers/genetics , DNA, Helminth/genetics , Embryonic Development/genetics , Epidermis/embryology , Epidermis/enzymology , Female , Gene Deletion , Genes, Helminth , Inositol 1,4,5-Trisphosphate/metabolism , Morphogenesis , Ovulation/genetics , Phosphoinositide Phospholipase C/antagonists & inhibitors , Phosphoinositide Phospholipase C/genetics , RNA Interference , Signal Transduction
2.
J Cell Biol ; 167(2): 231-44, 2004 Oct 25.
Article in English | MEDLINE | ID: mdl-15492045

ABSTRACT

In Saccharomyces cerevisiae, spindle orientation is controlled by a temporal and spatial program of microtubule (MT)-cortex interactions. This program requires Bud6p/Aip3p to direct the old pole to the bud and confine the new pole to the mother cell. Bud6p function has been linked to Kar9p, a protein guiding MTs along actin cables. Here, we show that Kar9p does not mediate Bud6p functions in spindle orientation. Based on live microscopy analysis, kar9Delta cells maintained Bud6p-dependent MT capture. Conversely, bud6Delta cells supported Kar9p-associated MT delivery to the bud. Moreover, additive phenotypes in bud6Delta kar9Delta or bud6Delta dyn1Delta mutants underscored the separate contributions of Bud6p, Kar9p, and dynein to spindle positioning. Finally, tub2C354S, a mutation decreasing MT dynamics, suppressed a kar9Delta mutation in a BUD6-dependent manner. Thus, Kar9p-independent capture at Bud6p sites can effect spindle orientation provided MT turnover is reduced. Together, these results demonstrate Bud6p function in MT capture at the cell cortex, independent of Kar9p-mediated MT delivery along actin cables.


Subject(s)
Microfilament Proteins/physiology , Microtubules/ultrastructure , Nuclear Proteins/physiology , Saccharomyces cerevisiae Proteins/physiology , Saccharomyces cerevisiae/metabolism , Spindle Apparatus , Actins/chemistry , Actins/metabolism , Cytoskeleton/metabolism , Dyneins/physiology , Fungal Proteins/chemistry , Green Fluorescent Proteins/metabolism , Microscopy, Fluorescence , Microtubule Proteins/chemistry , Models, Biological , Mutation , Phenotype , Plasmids/metabolism , Time Factors
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