ArticleNature communications2022
A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Erasing marks: Functions of plant deubiquitylating enzymes in modulating the ubiquitin code.The Plant cell · 2024Review
- A strategy for orthogonal deubiquitination using a bump-and-hole approach.RSC chemical biology · 2023Article
- Review
- Strategies for Monitoring "Ubiquitin C-Terminal Hydrolase 1" (Yuh1) Activity.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A widely distributed family of eukaryotic and bacterial deubiquitinases related to herpesviral large tegument proteins.Nature communications · 2022Article
- Lipid-mediated activation of plasma membrane-localized deubiquitylating enzymes modulate endosomal trafficking.Nature communications · 2022Article
- The emerging roles of deubiquitinases in plant proteostasis.Essays in biochemistry · 2022Review
- On the Study of Deubiquitinases: Using the Right Tools for the Job.Biomolecules · 2022Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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