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- W2971389287 abstract "Summary Prion-like proteins can assume distinct conformational and physical states in the same cell. Sequence analysis suggests that prion-like proteins are prevalent in various species; however, it remains unclear what functional space they occupy in multicellular organisms. Here, we report the identification of a prion-like protein, Herzog (CG5830), through a multimodal screen in Drosophila melanogaster. Herzog functions as a membrane-associated phosphatase and controls embryonic patterning, likely being involved in TGF-β/BMP and FGF/EGF signaling pathways. Remarkably, monomeric Herzog is enzymatically inactive and becomes active upon amyloid-like assembly. The prion-like domain of Herzog is necessary for both its assembly and membrane targeting. Removal of the prion-like domain impairs activity, while restoring assembly on the membrane using a heterologous prion-like domain and membrane-targeting motif can restore phosphatase activity. This study provides an example of a prion-like domain that allows an enzyme to gain essential functionality via amyloid-like assembly to control animal development." @default.
- W2971389287 created "2019-09-12" @default.
- W2971389287 creator A5010757951 @default.
- W2971389287 creator A5025842894 @default.
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- W2971389287 creator A5072100245 @default.
- W2971389287 creator A5074105995 @default.
- W2971389287 creator A5079994995 @default.
- W2971389287 date "2019-10-01" @default.
- W2971389287 modified "2023-09-28" @default.
- W2971389287 title "Amyloid-like Assembly Activates a Phosphatase in the Developing Drosophila Embryo" @default.
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