Resilin matrix distribution, variability and function in Drosophila
Abstract Background Elasticity prevents fatigue of tissues that are extensively and repeatedly deformed. Resilin is a resilient and elastic extracellular protein matrix in joints and hinges of insects. For its mechanical properties, Resilin is extensively analysed and applied in biomaterial and biom...
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BMC
2020-12-01
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Online Access: | https://doi.org/10.1186/s12915-020-00902-4 |
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author | Steven Lerch Renata Zuber Nicole Gehring Yiwen Wang Barbara Eckel Klaus-Dieter Klass Fritz-Olaf Lehmann Bernard Moussian |
author_facet | Steven Lerch Renata Zuber Nicole Gehring Yiwen Wang Barbara Eckel Klaus-Dieter Klass Fritz-Olaf Lehmann Bernard Moussian |
author_sort | Steven Lerch |
collection | DOAJ |
description | Abstract Background Elasticity prevents fatigue of tissues that are extensively and repeatedly deformed. Resilin is a resilient and elastic extracellular protein matrix in joints and hinges of insects. For its mechanical properties, Resilin is extensively analysed and applied in biomaterial and biomedical sciences. However, there is only indirect evidence for Resilin distribution and function in an insect. Commonly, the presence of dityrosines that covalently link Resilin protein monomers (Pro-Resilin), which are responsible for its mechanical properties and fluoresce upon UV excitation, has been considered to reflect Resilin incidence. Results Using a GFP-tagged Resilin version, we directly identify Resilin in pliable regions of the Drosophila body, some of which were not described before. Interestingly, the amounts of dityrosines are not proportional to the amounts of Resilin in different areas of the fly body, arguing that the mechanical properties of Resilin matrices vary according to their need. For a functional analysis of Resilin matrices, applying the RNA interference and Crispr/Cas9 techniques, we generated flies with reduced or eliminated Resilin function, respectively. We find that these flies are flightless but capable of locomotion and viable suggesting that other proteins may partially compensate for Resilin function. Indeed, localizations of the potentially elastic protein Cpr56F and Resilin occasionally coincide. Conclusions Thus, Resilin-matrices are composite in the way that varying amounts of different elastic proteins and dityrosinylation define material properties. Understanding the biology of Resilin will have an impact on Resilin-based biomaterial and biomedical sciences. |
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issn | 1741-7007 |
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spelling | doaj.art-5ffa3b87e1454a6fb1052b811e97973e2022-12-21T19:01:42ZengBMCBMC Biology1741-70072020-12-0118111510.1186/s12915-020-00902-4Resilin matrix distribution, variability and function in DrosophilaSteven Lerch0Renata Zuber1Nicole Gehring2Yiwen Wang3Barbara Eckel4Klaus-Dieter Klass5Fritz-Olaf Lehmann6Bernard Moussian7Applied Zoology, Technical University of DresdenApplied Zoology, Technical University of DresdenAnimal Genetics, Interfaculty Institute of Cell Biology, University of TübingenAnimal Genetics, Interfaculty Institute of Cell Biology, University of TübingenApplied Zoology, Technical University of DresdenSenckenberg Natural History CollectionsAnimal Physiology, University of RostockApplied Zoology, Technical University of DresdenAbstract Background Elasticity prevents fatigue of tissues that are extensively and repeatedly deformed. Resilin is a resilient and elastic extracellular protein matrix in joints and hinges of insects. For its mechanical properties, Resilin is extensively analysed and applied in biomaterial and biomedical sciences. However, there is only indirect evidence for Resilin distribution and function in an insect. Commonly, the presence of dityrosines that covalently link Resilin protein monomers (Pro-Resilin), which are responsible for its mechanical properties and fluoresce upon UV excitation, has been considered to reflect Resilin incidence. Results Using a GFP-tagged Resilin version, we directly identify Resilin in pliable regions of the Drosophila body, some of which were not described before. Interestingly, the amounts of dityrosines are not proportional to the amounts of Resilin in different areas of the fly body, arguing that the mechanical properties of Resilin matrices vary according to their need. For a functional analysis of Resilin matrices, applying the RNA interference and Crispr/Cas9 techniques, we generated flies with reduced or eliminated Resilin function, respectively. We find that these flies are flightless but capable of locomotion and viable suggesting that other proteins may partially compensate for Resilin function. Indeed, localizations of the potentially elastic protein Cpr56F and Resilin occasionally coincide. Conclusions Thus, Resilin-matrices are composite in the way that varying amounts of different elastic proteins and dityrosinylation define material properties. Understanding the biology of Resilin will have an impact on Resilin-based biomaterial and biomedical sciences.https://doi.org/10.1186/s12915-020-00902-4ResilinCuticleExtracellular matrixDrosophilaFlight |
spellingShingle | Steven Lerch Renata Zuber Nicole Gehring Yiwen Wang Barbara Eckel Klaus-Dieter Klass Fritz-Olaf Lehmann Bernard Moussian Resilin matrix distribution, variability and function in Drosophila BMC Biology Resilin Cuticle Extracellular matrix Drosophila Flight |
title | Resilin matrix distribution, variability and function in Drosophila |
title_full | Resilin matrix distribution, variability and function in Drosophila |
title_fullStr | Resilin matrix distribution, variability and function in Drosophila |
title_full_unstemmed | Resilin matrix distribution, variability and function in Drosophila |
title_short | Resilin matrix distribution, variability and function in Drosophila |
title_sort | resilin matrix distribution variability and function in drosophila |
topic | Resilin Cuticle Extracellular matrix Drosophila Flight |
url | https://doi.org/10.1186/s12915-020-00902-4 |
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