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The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila
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 uns...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440989/ https://www.ncbi.nlm.nih.gov/pubmed/30926832 http://dx.doi.org/10.1038/s41598-019-41734-9 |
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author | Zuber, Renata Shaik, Khaleelulla Saheb Meyer, Frauke Ho, Hsin-Nin Speidel, Anna Gehring, Nicole Bartoszewski, Slawomir Schwarz, Heinz Moussian, Bernard |
author_facet | Zuber, Renata Shaik, Khaleelulla Saheb Meyer, Frauke Ho, Hsin-Nin Speidel, Anna Gehring, Nicole Bartoszewski, Slawomir Schwarz, Heinz Moussian, Bernard |
author_sort | Zuber, Renata |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6440989 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-64409892019-04-04 The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila Zuber, Renata Shaik, Khaleelulla Saheb Meyer, Frauke Ho, Hsin-Nin Speidel, Anna Gehring, Nicole Bartoszewski, Slawomir Schwarz, Heinz Moussian, Bernard Sci Rep Article 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. Nature Publishing Group UK 2019-03-29 /pmc/articles/PMC6440989/ /pubmed/30926832 http://dx.doi.org/10.1038/s41598-019-41734-9 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Zuber, Renata Shaik, Khaleelulla Saheb Meyer, Frauke Ho, Hsin-Nin Speidel, Anna Gehring, Nicole Bartoszewski, Slawomir Schwarz, Heinz Moussian, Bernard The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila |
title | The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila |
title_full | The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila |
title_fullStr | The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila |
title_full_unstemmed | The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila |
title_short | The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila |
title_sort | putative c-type lectin schlaff ensures epidermal barrier compactness in drosophila |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440989/ https://www.ncbi.nlm.nih.gov/pubmed/30926832 http://dx.doi.org/10.1038/s41598-019-41734-9 |
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