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• W4205124495 abstract "Eukaryotic deubiquitinases are important regulators of ubiquitin signaling and can be subdivided into several structurally distinct classes. The ZUFSP family, with ZUP1 as its sole human member, has a modular architecture with a core catalytic domain highly active against the ubiquitin-derived peptide RLRGG, but not against ubiquitin itself. Ubiquitin recognition is conferred by additional non-catalytic domains, making full-length ZUP1 active against long K63-linked chains. However, non-mammalian ZUFSP family members contain different ubiquitin-binding domains in their N-terminal regions, despite their high conservation within the catalytic domain. Here, by working with representative ZUFSP family members from insects, fungi and plants, we show that different N-terminal domains are associated with different linkage preferences. Biochemical and structural studies suggest that the acquisition of two family-specific proximal domains have changed the default K48 preference of the ZUFSP family to the K63 preference observed in ZUP1 and its insect homolog. Additional N-terminal zinc finger domains promote chain cleavage without changing linkage-specificity." @default.
• W4205124495 created "2022-01-26" @default.
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• W4205124495 date "2022-01-20" @default.
• W4205124495 modified "2023-10-09" @default.
• W4205124495 title "A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family" @default.
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• W4205124495 doi "https://doi.org/10.1038/s41467-022-28049-6" @default.
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