| one publication added to basket [361744] | In the footsteps of sea stars: deciphering the catalogue of proteins involved in underwater temporary adhesion
Algrain, M.; Hennebert, E.; Bertemes, P.; Wattiez, R.; Flammang, P.; Lengerer, B. (2022). In the footsteps of sea stars: deciphering the catalogue of proteins involved in underwater temporary adhesion. Open Biology 12(8): 220103. https://dx.doi.org/10.1098/rsob.220103
In: Open Biology. Royal Society: London. e-ISSN 2046-2441, meer
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| Trefwoorden |
Asterias rubens Linnaeus, 1758 [WoRMS]; Asteroidea [WoRMS]; Echinodermata [WoRMS]
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| Author keywords |
Echinodermata; Asteroidea; tube feet; sea star footprint protein; duo-gland adhesive system; proteomics and transcriptomics |
| Auteurs | | Top |
- Algrain, M., meer
- Hennebert, E., meer
- Bertemes, P.
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| Abstract |
Sea stars adhere strongly but temporarily to underwater substrata via the secretion of a blend of proteins, forming an adhesive footprint that they leave on the surface after detachment. Their tube feet enclose a duo-gland adhesive system comprising two types of adhesive cells, contributing different layers of the footprint and de-adhesive cells. In this study, we characterized the catalogue of sea star footprint proteins (Sfps) in the species Asterias rubens to gain insights in their potential function. We identified 16 Sfps and mapped their expression to type 1 and/or type 2 adhesive cells or to de-adhesive cells by double fluorescent in situ hybridization. Based on their cellular expression pattern and their conserved functional domains, we propose that the identified Sfps serve different functions during attachment, with two Sfps coupling to the surface, six providing cohesive strength and the rest forming a binding matrix. Immunolabelling of footprints with antibodies directed against one protein of each category confirmed these roles. A de-adhesive gland cell-specific astacin-like proteinase presumably weakens the bond between the adhesive material and the tube foot surface during detachment. Overall, we provide a model for temporary adhesion in sea stars, including a comprehensive list of the proteins involved. |
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