| Autor: |
Berenice Ziegler, Irene Yiallouros, Benjamin Trageser, Sumit Kumar, Moritz Mercker, Svenja Kling, Maike Fath, Uwe Warnken, Martina Schnölzer, Thomas W. Holstein, Markus Hartl, Anna Marciniak-Czochra, Jörg Stetefeld, Walter Stöcker, Suat Özbek |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
BMC Biology, Vol 19, Iss 1, Pp 1-22 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
1741-7007 |
| DOI: |
10.1186/s12915-021-01046-9 |
| Popis: |
Abstract Background The Hydra head organizer acts as a signaling center that initiates and maintains the primary body axis in steady state polyps and during budding or regeneration. Wnt/beta-Catenin signaling functions as a primary cue controlling this process, but how Wnt ligand activity is locally restricted at the protein level is poorly understood. Here we report a proteomic analysis of Hydra head tissue leading to the identification of an astacin family proteinase as a Wnt processing factor. Results Hydra astacin-7 (HAS-7) is expressed from gland cells as an apical-distal gradient in the body column, peaking close beneath the tentacle zone. HAS-7 siRNA knockdown abrogates HyWnt3 proteolysis in the head tissue and induces a robust double axis phenotype, which is rescued by simultaneous HyWnt3 knockdown. Accordingly, double axes are also observed in conditions of increased Wnt activity as in transgenic actin::HyWnt3 and HyDkk1/2/4 siRNA treated animals. HyWnt3-induced double axes in Xenopus embryos could be rescued by coinjection of HAS-7 mRNA. Mathematical modelling combined with experimental promotor analysis indicate an indirect regulation of HAS-7 by beta-Catenin, expanding the classical Turing-type activator-inhibitor model. Conclusions We show the astacin family protease HAS-7 maintains a single head organizer through proteolysis of HyWnt3. Our data suggest a negative regulatory function of Wnt processing astacin proteinases in the global patterning of the oral-aboral axis in Hydra. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
