Sticky worms: adhesion complexes in<i>C. elegans</i>

Cox, Elisabeth A.; Hardin, Jeff

doi:10.1242/jcs.01176

Cited by 82 publications

(70 citation statements)

References 126 publications

(166 reference statements)

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“…One is to attach the epidermis to the ECM and maintain epidermis integrity; the other is to act as tendon-like structures that transmit muscle tension to the cuticle exoskeleton. Similar structures are present in the pharynx marginal epithelial cells, rectum, vulva, and in areas of the epidermis that contact the mechanosensory touch neurons (Cox and Hardin, 2004). As detailed below, there are some differences between the hemidesmosome-like junctions found apically and basally.…”

Section: Developmental Dynamicsmentioning

confidence: 84%

The making of hemidesmosome structures in vivo

Zhang

Labouesse

2010

Developmental Dynamics

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Hemidesmosomes are evolutionarily conserved attachment complexes linked to intermediate filaments that connect epithelial cells to the extracellular matrix. They provide tissue integrity and resistance to mechanical forces. Alterations in hemidesmosome structures are responsible for skin blistering, carcinoma invasion, and wound-healing defects. Valuable information about hemidesmosome assembly and disassembly has been obtained from in vitro cell culture studies. However, how these processes take place in vivo still remains elusive. Here, we discuss recent data about the formation and reorganization of hemidesmosomes in several in vivo model systems, particularly zebrafish and Caenorhabditis elegans, focusing on various factors affecting their dynamics. Mechanisms found in different organisms reveal that hemidesmosome formation and maintenance in vivo are carefully controlled by ECM protein folding, ECM-receptor expression and trafficking, and by post-translational modification of hemidesmosome components. These findings validate and extend the in vitro studies, and shed light on our understanding about hemidesmosomes across species.

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Section: Developmental Dynamicsmentioning

confidence: 84%

The making of hemidesmosome structures in vivo

Zhang

Labouesse

2010

Developmental Dynamics

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“…3, D and E). Fibrous organelles are composed of intermediate filament arrays that associate with the cuticle, muscle, and neurons (36). To confirm the ER localization we generated a double transgenic strain that expressed the ER marker TRAM (translocating chain-associated membrane) protein fused to mCherry from the hypodermal promoter dyp-7 (37) and hrg-2::HRG-2-YFP.…”

Section: Heme Deficiency Induces the Expression Of Hrg-2 In C Elegans-mentioning

confidence: 99%

Heme Utilization in the Caenorhabditis elegans Hypodermal Cells Is Facilitated by Heme-responsive Gene-2

Chen

Samuel

Krause

et al. 2012

Journal of Biological Chemistry

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“…These structures have been thoroughly studied using a combination of biochemical and genetic approaches that have shed light on their composition (Waterston, 1988;Moerman and Williams, 2006). Dense bodies are themselves anchored to the muscle cell and basement membrane via specialized proteins, all of which are also known components of vertebrate focal adhesion plaques (reviewed in Cox and Hardin, 2004;Labouesse and Georges-Labouesse, 2003;Lecroisey et al, 2007).…”

Section: Subcellular Localization Of Dyc-1mentioning

confidence: 99%

DYC-1, a Protein Functionally Linked to Dystrophin inCaenorhabditis elegansIs Associated with the Dense Body, Where It Interacts with the Muscle LIM Domain Protein ZYX-1

Lecroisey

Martin

Mariol

et al. 2008

MBoC

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In Caenorhabditis elegans, mutations of the dystrophin homologue, dys-1, produce a peculiar behavioral phenotype (hyperactivity and a tendency to hypercontract). In a sensitized genetic background, dys-1 mutations also lead to muscle necrosis. The dyc-1 gene was previously identified in a genetic screen because its mutation leads to the same phenotype as dys-1, suggesting that the two genes are functionally linked. Here, we report the detailed characterization of the dyc-1 gene. dyc-1 encodes two isoforms, which are expressed in neurons and muscles. Isoform-specific RNAi experiments show that the absence of the muscle isoform, and not that of the neuronal isoform, is responsible for the dyc-1 mutant phenotype. In the sarcomere, the DYC-1 protein is localized at the edges of the dense body, the nematode muscle adhesion structure where actin filaments are anchored and linked to the sarcolemma. In yeast two-hybrid assays, DYC-1 interacts with ZYX-1, the homologue of the vertebrate focal adhesion LIM domain protein zyxin. ZYX-1 localizes at dense bodies and M-lines as well as in the nucleus of C. elegans striated muscles. The DYC-1 protein possesses a highly conserved 19 amino acid sequence, which is involved in the interaction with ZYX-1 and which is sufficient for addressing DYC-1 to the dense body. Altogether our findings indicate that DYC-1 may be involved in dense body function and stability. This, taken together with the functional link between the C. elegans DYC-1 and DYS-1 proteins, furthermore suggests a requirement of dystrophin function at this structure. As the dense body shares functional similarity with both the vertebrate Z-disk and the costamere, we therefore postulate that disruption of muscle cell adhesion structures might be the primary event of muscle degeneration occurring in the absence of dystrophin, in C. elegans as well as vertebrates.

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Sticky worms: adhesion complexes inC. elegans

Cited by 82 publications

References 126 publications

The making of hemidesmosome structures in vivo

The making of hemidesmosome structures in vivo

Heme Utilization in the Caenorhabditis elegans Hypodermal Cells Is Facilitated by Heme-responsive Gene-2

DYC-1, a Protein Functionally Linked to Dystrophin inCaenorhabditis elegansIs Associated with the Dense Body, Where It Interacts with the Muscle LIM Domain Protein ZYX-1

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