scholarly journals C. elegans daf-6 Encodes a Patched-Related Protein Required for Lumen Formation

2005 ◽  
Vol 8 (6) ◽  
pp. 893-906 ◽  
Author(s):  
Elliot A. Perens ◽  
Shai Shaham
Keyword(s):  
Related Protein ◽  
Lumen Formation ◽  
C Elegans

The Caenorhabditis elegans odr-2 Gene Encodes a Novel Ly-6-Related Protein Required for Olfaction

Genetics ◽  
2001 ◽  
Vol 157 (1) ◽  
pp. 211-224 ◽  
Author(s):  
Joseph H Chou ◽  
Cornelia I Bargmann ◽  
Piali Sengupta
Keyword(s):  
Caenorhabditis Elegans ◽  
Motor Neurons ◽  
Amino Terminus ◽  
Signaling Proteins ◽  
Related Protein ◽  
Olfactory Neurons ◽  
Unique Role ◽  
C Elegans ◽  
Founding Member ◽  
High Concentrations

Abstract Caenorhabditis elegans odr-2 mutants are defective in the ability to chemotax to odorants that are recognized by the two AWC olfactory neurons. Like many other olfactory mutants, they retain responses to high concentrations of AWC-sensed odors; we show here that these residual responses are caused by the ability of other olfactory neurons (the AWA neurons) to be recruited at high odor concentrations. odr-2 encodes a membrane-associated protein related to the Ly-6 superfamily of GPI-linked signaling proteins and is the founding member of a C. elegans gene family with at least seven other members. Alternative splicing of odr-2 yields three predicted proteins that differ only at the extreme amino terminus. The three isoforms have different promoters, and one isoform may have a unique role in olfaction. An epitope-tagged ODR-2 protein is expressed at high levels in sensory neurons, motor neurons, and interneurons and is enriched in axons. The AWC neurons are superficially normal in their development and structure in odr-2 mutants, but their function is impaired. Our results suggest that ODR-2 may regulate AWC signaling within the neuronal network required for chemotaxis.

scholarly journals The Agrin/Perlecan-Related Protein Eyes Shut Is Essential for Epithelial Lumen Formation in the Drosophila Retina

2006 ◽  
Vol 11 (4) ◽  
pp. 483-493 ◽  
Author(s):  
Nicole Husain ◽  
Milena Pellikka ◽  
Henry Hong ◽  
Tsveta Klimentova ◽  
Kwang-Min Choe ◽  
...  
Keyword(s):  
Related Protein ◽  
Lumen Formation

scholarly journals Regulation of Membrane Trafficking by a Novel Cdc42-related Protein in Caenorhabditis elegans Epithelial Cells

2005 ◽  
Vol 16 (4) ◽  
pp. 1629-1639 ◽  
Author(s):  
S. Jenna ◽  
M.-E. Caruso ◽  
A. Emadali ◽  
D. T. Nguyên ◽  
M. Dominguez ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Epithelial Cells ◽  
Membrane Trafficking ◽  
Rho Gtpases ◽  
Related Protein ◽  
Recycling Endosomes ◽  
C Elegans ◽  
Apical Trafficking ◽  
Golgi Network

Rho GTPases are mainly known for their implication in cytoskeleton remodeling. They have also been recently shown to regulate various aspects of membrane trafficking. Here, we report the identification and the characterization of a novel Caenorhabditis elegans Cdc42-related protein, CRP-1, that shows atypical enzymatic characteristics in vitro. Expression in mouse fibroblasts revealed that, in contrast with CDC-42, CRP-1 was unable to reorganize the actin cytoskeleton and mainly localized to trans-Golgi network and recycling endosomes. This subcellular localization, as well as its expression profile restricted to a subset of epithelial-like cells in C. elegans, suggested a potential function for this protein in polarized membrane trafficking. Consistent with this hypothesis, alteration of CRP-1 expression affected the apical trafficking of CHE-14 in vulval and rectal epithelial cells and sphingolipids (C6-NBD-ceramide) uptake and/or trafficking in intestinal cells. However, it did not affect basolateral trafficking of myotactin in the pharynx and the targeting of IFB-2 and AJM-1, two cytosolic apical markers of intestine epithelial cells. Hence, our data demonstrate a function for CRP-1 in the regulation of membrane trafficking in a subset of cells with epithelial characteristics.

scholarly journals Perilipin-related protein regulates lipid metabolism in C. elegans

2015 ◽  
Author(s):  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Markéta Kostrouchová ◽  
Jan Philipp Novotný ◽  
Michael W. Krause ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplets ◽  
Fat Metabolism ◽  
Droplet Surface ◽  
Surface Proteins ◽  
Related Protein ◽  
Additional Mechanism ◽  
C Elegans ◽  
Functional Studies ◽  
Gene Inhibition

The perilipins are lipid droplet surface proteins that contribute to fat metabolism by controlling the access of lipids to lipolytic enzymes. Perilipins have been identified in organisms as diverse as metazoa, fungi, and amoebas but strikingly not in nematodes. Here we identify the protein encoded by the W01A8.1 gene in Caenorhabditis elegans as the closest homologue of metazoan perilipin. We demonstrate that nematode W01A8.1 is a cytoplasmic protein residing on lipid droplets. Human perilipins 1 and 2 localize in transgenic C. elegans on the same structures as proteins expressed from W01A8.1 gene. Inhibition and elimination of W01A8.1 affects the appearance of lipid droplets especially visible as the formation of large lipid droplets localized around the dividing nucleus during the early zygotic divisions. This phenomenon disappears in later stages of embryogenesis indicating the existence of an additional mechanism of lipid regulation in C. elegans. Our results demonstrate that perilipin-related regulation of fat metabolism is conserved in nematodes and provide new possibilities for functional studies of lipid metabolism.

scholarly journals Clathrin and AP-1 regulate apical polarity and lumen formation during C. elegans tubulogenesis

Development ◽  
2012 ◽  
Vol 139 (11) ◽  
pp. 2071-2083 ◽  
Author(s):  
H. Zhang ◽  
A. Kim ◽  
N. Abraham ◽  
L. A. Khan ◽  
D. H. Hall ◽  
...  
Keyword(s):  
Lumen Formation ◽  
C Elegans ◽  
Apical Polarity

scholarly journals Multi-tissue patterning drives anterior morphogenesis of the C. elegans embryo

2020 ◽  
Author(s):  
Stephanie Grimbert ◽  
Karina Mastronardi ◽  
Ryan Christensen ◽  
Christopher Law ◽  
David Fay ◽  
...  
Keyword(s):  
Epidermal Cells ◽  
Model Organisms ◽  
Complex Structures ◽  
Lumen Formation ◽  
C Elegans ◽  
The Future ◽  
Embryonic Morphogenesis ◽  
And Control ◽  
Different Tissues

AbstractComplex structures derived from multiple tissue types are challenging to study in vivo, and our knowledge of how cells from different tissues are coordinated is limited. Model organisms have proven invaluable for improving our understanding of how chemical and mechanical cues between cells from two different tissues can govern specific morphogenetic events. Here we used Caenorhabditis elegans as a model system to show how cells from three different tissues are coordinated to give rise to the anterior lumen. This poorly understood process has remained a black box for embryonic morphogenesis. Using various microscopy and software approaches, we describe the movements and patterns of epidermal cells, neuroblasts and pharyngeal cells that contribute to lumen formation. The anterior-most pharyngeal cells (arcade cells) may provide the first marker for the location of the future lumen and facilitate the patterning of the surrounding neuroblasts. These neuroblast patterns control the rate of migration of the anterior epidermal cells, whereas the epidermal cells ultimately reinforce and control the position of the future lumen, as they must join with the pharyngeal cells for their epithelialization. Our studies are the first to characterize anterior morphogenesis in C. elegans in detail and should lay the framework for identifying how these different patterns are controlled at the molecular level.

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