cut-1 a Caenorhabditis elegans gene coding for a dauer-specific noncollagenous component of the cuticle

Sebastiano, Marisa; Lassandro, Francesco; Bazzicalupo, Paolo

doi:10.1016/0012-1606(91)90253-y

Cited by 77 publications

(54 citation statements)

References 17 publications

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“…One member of this family, the product of the C. elegans cuticulin-1 gene (cut-1), has been identified as a structural component of the most external part of the worm cuticle (Sebastiano et al, 1991). Here we show that the m gene also encodes a ZP protein.…”

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confidence: 78%

“…One of the C. elegans proteins containing a ZP domain, Cut-1, has been identified as a structural component of the nematode cuticle. Cut-1 protein is apically secreted and localises in the most external cuticle layer, the cuticulin (Sebastiano et al, 1991). In the Drosophila wing, the epidermal cells secrete the cuticulin envelope prior to the reorganisation of the apical membrane that takes place during differentiation.…”

Section: Discussionmentioning

confidence: 99%

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Drosophila miniatureandduskyencode ZP proteins required for cytoskeletal reorganisation during wing morphogenesis

Roch

Alonso

Akam

2003

Journal of Cell Science

117

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We have characterised the function of two Drosophila genes, miniature and dusky, that are required for the morphological reorganisation of the apical membrane during wing epidermis differentiation. These genes encode transmembrane proteins containing a ZP (zona pellucida)domain and are homologous to several vertebrate and invertebrate apical matrix components. miniature and dusky are only expressed in tissues secreting a cuticle, and the Min protein localises to the apical membrane during the early stages of cuticle formation. We propose that Min and Dusky form a novel subfamily within the ZP domain proteins and are specifically involved in the interactions between the apical membrane, the cytoskeleton and the forming cuticle.

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mentioning

confidence: 78%

Section: Discussionmentioning

confidence: 99%

Drosophila miniatureandduskyencode ZP proteins required for cytoskeletal reorganisation during wing morphogenesis

Roch

Alonso

Akam

2003

Journal of Cell Science

117

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“…Such aECMs may serve as protective barriers against environmental influences, provide apical attachment sites for the underlying epithelium, or temporarily assist in epithelial remodelling (Sebastiano et al, 1991;Jovine et al, 2002;Roch et al, 2003;Bökel et al, 2005;Moussian and Uv, 2005). Apical ECMs are rich in carbohydrates such as glucosaminoglycans and glycosyl-groups on proteins.…”

Section: Introductionmentioning

confidence: 99%

Hormonal regulation ofmummyis needed for apical extracellular matrix formation and epithelial morphogenesis inDrosophila

et al. 2006

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Many epithelia produce apical extracellular matrices (aECM) that are crucial for organ morphogenesis or physiology. Apical ECM formation relies on coordinated synthesis and modification of constituting components, to enable their subcellular targeting and extracellular assembly into functional matrices. The exoskeleton of Drosophila, the cuticle, is a stratified aECM containing ordered chitin polysaccharide lamellae and proteinaceous layers, and is suited for studies of molecular functions needed for aECM assembly. Here, we show that Drosophila mummy (mmy) mutants display defects in epithelial organisation in conjunction with aberrant deposition of the cuticle and an apical matrix needed for tracheal tubulogenesis. We find that mmy encodes the UDP-Nacetylglucosamine pyrophosphorylase, which catalyses the production of UDP-N-acetylglucosamine, an obligate substrate for chitin synthases as well as for protein glycosylation and GPI-anchor formation. Consequently, in mmy mutants GlcNAc-groups including chitin are severely reduced and modification and subcellular localisation of proteins designated for extracellular space is defective. Moreover, mmy expression is selectively upregulated in epithelia at the time they actively deposit aECM, and is altered by the moulting hormone 20-Hydroxyecdysone, suggesting that mmy is part of a developmental genetic programme to promote aECM formation.

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“…Its major components are collagen-like proteins which can be extracted by a combination of strong ionic detergents and disulphide reducing agents. Cuticlin, the insoluble residue left after extraction, is resistant to collagenase and consists of a highly cross-linked mixture of different proteins.We have previously identified two genes, cut-1 and cut-2, coding for components of the insoluble cuticlin residue of the free living nematode Caenorhabditis elegans [1,2]. The cloned genes have provided the opportunity to obtain recombinant cuticlin proteins.…”

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confidence: 99%

Structural analysis of ASCUT‐1, a protein component of the cuticle of the parasitic nematode Ascaris lumbricoides

D’Auria

Rossi

Tanfani

et al. 1998

European Journal of Biochemistry

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CUT-1 from the intestinal parasitic nematode Ascaris lumbricoides is a protein component of the insoluble residue of the cuticle, cuticlin. It contains the CUT-1-like domain which is shared by members of a novel family of components of extracellular matrices. The structure and the thermal stability of recombinant CUT-1 from A. lumbricoides (ASCUT-1) were investigated by Fourier-transform infrared (FT-IR) and CD spectroscopy. The data revealed that the secondary structure of the protein at 20°C, both as insoluble inclusion bodies or in soluble form, contains about 50% β structure, 14% A-helix and 25% turns. A tendency of A. lumbricoides CUT-1 to form aggregates was documented by FT-IR spectroscopy which showed also that the addition of SDS disrupts these interactions. Near-ultraviolet CD spectra confirmed these data and suggested that phenylalanine residues are probably involved in intermolecular hydrophobic interactions responsible for the tendency of the protein to aggregate. Near-ultraviolet spectra showed also that part of the cysteine residues forms disulphide bridges responsible for the tertiary architecture of the protein. Finally, FT-IR and CD data revealed that ASCUT-1 is very stable at high temperatures. This stability and the tendency of ASCUT-1 to form aggregates suggest that these properties may be important for a protein which is a component of a particularly resistant extracellular matrix such as the nematode cuticle.Keywords : nematode cuticle; inclusion bodies ; circular dichroism ; Fourier-transform infrared spectroscopy; recombinant protein.The nematode cuticle is a multilayered elastic extracellular structure which surrounds the animal and functions as an exoskeleton, determining the body shape of the worm. Its major components are collagen-like proteins which can be extracted by a combination of strong ionic detergents and disulphide reducing agents. Cuticlin, the insoluble residue left after extraction, is resistant to collagenase and consists of a highly cross-linked mixture of different proteins.We have previously identified two genes, cut-1 and cut-2, coding for components of the insoluble cuticlin residue of the free living nematode Caenorhabditis elegans [1,2]. The cloned genes have provided the opportunity to obtain recombinant cuticlin proteins. In particular, it has been possible for the first time to study some aspects of the mechanism of CUT-2 cross-linking [3]. In addition, specific antibodies have been raised against the recombinant proteins and have been used to localise the corresponding proteins within the cuticle layers [4,5]. While CUT-2 is a component of the cuticle of all stages of C. elegans [2], CUT-1 is present only in the cuticle of dauer larvae where it forms two ribbons running the whole length of the worm, underneath the lateral alae The two genes represent two different families of cuticlin components. CUT-2 shares similarity with a group of insect proteins which also participate in the formation of extracellular protective structures such as the egg-shell layers [...

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cut-1 a Caenorhabditis elegans gene coding for a dauer-specific noncollagenous component of the cuticle

Cited by 77 publications

References 17 publications

Drosophila miniatureandduskyencode ZP proteins required for cytoskeletal reorganisation during wing morphogenesis

Drosophila miniatureandduskyencode ZP proteins required for cytoskeletal reorganisation during wing morphogenesis

Hormonal regulation ofmummyis needed for apical extracellular matrix formation and epithelial morphogenesis inDrosophila

Structural analysis of ASCUT‐1, a protein component of the cuticle of the parasitic nematode Ascaris lumbricoides

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