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 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 plakin Short Stop and the RhoA GTPase are required for E-cadherin-dependent apical surface remodeling during tracheal tube fusion

Development ◽  
2002 ◽  
Vol 129 (6) ◽  
pp. 1509-1520 ◽  
Author(s):  
Seungbok Lee ◽  
Peter A. Kolodziej
Keyword(s):  
Drosophila Melanogaster ◽  
Apical Cell ◽  
Dominant Negative ◽  
Apical Surface ◽  
Lumen Formation ◽  
Rhoa Gtpase ◽  
Apical Polarity ◽  
Actin Structure ◽  
Surface Remodeling ◽  
E Cadherin

Cells in vascular and other tubular networks require apical polarity in order to contact each other properly and to form lumen. As tracheal branches join together in Drosophila melanogaster embryos, specialized cells at the junction form a new E-cadherin-based contact and assemble an associated track of F-actin and the plakin Short Stop (shot). In these fusion cells, the apical surface determinant Discs Lost (Dlt) is subsequently deposited and new lumen forms along the track. In shot mutant embryos, the fusion cells fail to remodel the initial E-cadherin contact, to make an associated F-actin structure and to form lumenal connections between tracheal branches. Shot binding to F-actin and microtubules is required to rescue these defects. This finding has led us to investigate whether other regulators of the F-actin cytoskeleton similarly affect apical cell surface remodeling and lumen formation. Expression of constitutively active RhoA in all tracheal cells mimics the shot phenotype and affects Shot localization in fusion cells. The dominant negative RhoA phenotype suggests that RhoA controls apical surface formation throughout the trachea. We therefore propose that in fusion cells, Shot may function downstream of RhoA to form E-cadherin-associated cytoskeletal structures that are necessary for apical determinant localization.

The apical polarity network in C. elegans larval epithelia

10.33540/822 ◽  
2021 ◽  
Author(s):  
◽  
María Victoria García Castiglioni
Keyword(s):  
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.

scholarly journals A polarity pathway for exocyst-dependent intracellular tube extension

2020 ◽  
Author(s):  
Joshua Abrams ◽  
Jeremy Nance
Keyword(s):  
Mammalian Cells ◽  
Rho Gtpase ◽  
Tube Formation ◽  
Membrane Domain ◽  
Lumen Formation ◽  
Vesicle Tethering ◽  
C Elegans ◽  
And Function ◽  
Excretory Cell ◽  
Upstream Regulators

ABSTRACTLumen extension in intracellular tubes can occur by the directed fusion of vesicles with an invading apical membrane domain. Within the C. elegans excretory cell, which contains an intracellular tube, the exocyst vesicle-tethering complex is enriched at the lumenal membrane domain and is required for tube formation, suggesting that it targets vesicles needed for lumen extension. Here, we identify a polarity pathway that promotes intracellular tube formation by enriching the exocyst at the lumenal membrane. We show that the PAR polarity proteins PAR-6 and PKC-3/aPKC localize to the lumenal membrane domain and function within the excretory cell to promote lumen extension, similar to exocyst component SEC-5 and exocyst regulator RAL-1. Using acute protein depletion, we find that PAR-6 is required to recruit the exocyst to the lumenal membrane domain, whereas PAR-3, which functions as an exocyst receptor in mammalian cells, appears to be dispensable for exocyst localization and lumen extension. Finally, we show that the Rho GTPase CDC-42 and the RhoGEF EXC-5/FGD act as upstream regulators of lumen formation by recruiting PAR-6 and PKC-3 to the lumenal membrane. Our findings reveal a molecular pathway that connects Rho GTPase signaling, cell polarity, and vesicle-tethering proteins to promote lumen extension in intracellular tubes.

scholarly journals ERM-1 phosphorylation and NRFL-1 redundantly control lumen formation in the C. elegans intestine

2021 ◽  
Author(s):  
Jorian J. Sepers ◽  
João J. Ramalho ◽  
Jason R. Kroll ◽  
Ruben Schmidt ◽  
Mike Boxem
Keyword(s):  
Pdz Domain ◽  
Actin Binding ◽  
Intestinal Lumen ◽  
Intestinal Development ◽  
Loss Of Function ◽  
Molecular Scaffolds ◽  
Lumen Formation ◽  
Erm Proteins ◽  
C Elegans ◽  
Apical Domain

AbstractReorganization of the plasma membrane and underlying actin cytoskeleton into specialized domains is essential for the functioning of most polarized cells in animals. Proteins of the ezrin-radixin-moesin (ERM) and Na+/H+ exchanger 3 regulating factor (NHERF) family are conserved regulators of cortical specialization. ERM proteins function as membrane-actin linkers and as molecular scaffolds that organize the distribution of proteins at the membrane. NHERF proteins are PDZ-domain containing adapters that can bind to ERM proteins and extend their scaffolding capability. Here, we investigate how ERM and NHERF proteins function in regulating intestinal lumen formation in the nematode Caenorhabditis elegans. C. elegans has single ERM and NHERF family proteins, termed ERM-1 and NRFL-1, and ERM-1 was previously shown to be critical for intestinal lumen formation. Using CRISPR/Cas9-generated nrfl-1 alleles we demonstrate that NRFL-1 localizes at the intestinal microvilli, and that this localization is depended on an interaction with ERM-1. However, nrfl-1 loss of function mutants are viable and do not show defect in intestinal development. Interestingly, combining nrfl-1 loss with erm-1 mutants that either block or mimic phosphorylation of a regulatory C-terminal threonine causes severe defects in intestinal lumen formation. These defects are not observed in the phosphorylation mutants alone, and resemble the effects of strong erm-1 loss of function. The loss of NRFL-1 did not affect the localization or activity of ERM-1. Together, these data indicate that ERM-1 and NRFL-1 function together in intestinal lumen formation in C. elegans. We postulate that the functioning of ERM-1 in this tissue involves actin-binding activities that are regulated by the C-terminal threonine residue and the organization of apical domain composition through NRFL-1.

scholarly journals De novo lumen formation and elongation in the developing nephron: a central role for afadin in apical polarity

Development ◽  
2013 ◽  
Vol 140 (8) ◽  
pp. 1774-1784 ◽  
Author(s):  
Z. Yang ◽  
S. Zimmerman ◽  
P. R. Brakeman ◽  
G. M. Beaudoin ◽  
L. F. Reichardt ◽  
...  
Keyword(s):  
De Novo ◽  
Lumen Formation ◽  
Apical Polarity

scholarly journals The anchor cell initiates dorsal lumen formation during C. elegans vulval tubulogenesis

2009 ◽  
Vol 328 (2) ◽  
pp. 297-304 ◽  
Author(s):  
Kathleen A. Estes ◽  
Wendy Hanna-Rose
Keyword(s):  
Lumen Formation ◽  
C Elegans ◽  
Anchor Cell

The glycomes of Caenorhabditis elegans and other model organisms

2002 ◽  
Vol 69 ◽  
pp. 117-134 ◽  
Author(s):  
Stuart M. Haslam ◽  
David Gems ◽  
Howard R. Morris ◽  
Anne Dell
Keyword(s):  
Caenorhabditis Elegans ◽  
Current Knowledge ◽  
Structural Data ◽  
Model Organisms ◽  
Entire Genome ◽  
C Elegans ◽  
The Face ◽  
Area Of Concern ◽  
Nematode Worm

There is no doubt that the immense amount of information that is being generated by the initial sequencing and secondary interrogation of various genomes will change the face of glycobiological research. However, a major area of concern is that detailed structural knowledge of the ultimate products of genes that are identified as being involved in glycoconjugate biosynthesis is still limited. This is illustrated clearly by the nematode worm Caenorhabditis elegans, which was the first multicellular organism to have its entire genome sequenced. To date, only limited structural data on the glycosylated molecules of this organism have been reported. Our laboratory is addressing this problem by performing detailed MS structural characterization of the N-linked glycans of C. elegans; high-mannose structures dominate, with only minor amounts of complex-type structures. Novel, highly fucosylated truncated structures are also present which are difucosylated on the proximal N-acetylglucosamine of the chitobiose core as well as containing unusual Fucα1–2Gal1–2Man as peripheral structures. The implications of these results in terms of the identification of ligands for genomically predicted lectins and potential glycosyltransferases are discussed in this chapter. Current knowledge on the glycomes of other model organisms such as Dictyostelium discoideum, Saccharomyces cerevisiae and Drosophila melanogaster is also discussed briefly.

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