ArticleScientific reports2019
The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Gene Expression During Scale Development in Pachyrhynchus Weevils.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2026Article
- Adaptive evolution of traits for parasitism and pathogen transmission potential in bat flies.National science review · 2025Article
- Proteomic analysis of pharate pupal molting fluid from the tobacco hornworm, Manduca sexta.Insect biochemistry and molecular biology · 2022Article
- Review
- A corset function of exoskeletal ECM promotes body elongation in Drosophila.Communications biology · 2021Article
- A New C-Type Lectin Homolog SpCTL6 Exerting Immunoprotective Effect and Regulatory Role in Mud CrabFrontiers in immunology · 2021Article
- Tweedle proteins form extracellular two-dimensional structures defining body and cell shape inOpen biology · 2020Article
- Form and function of the apical extracellular matrix: new insights fromFaculty reviews · 2020Review
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
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Abstract
The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a putative C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
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