ArticleScientific reports2019
The ubiquitin interacting motifs of USP37 act on the proximal Ub of a di-Ub chain to enhance catalytic efficiency.
Article in Scientific reports, 2019. 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, 16 citations in OpenAlex.
- Ubiquitin Engineering for Interrogating the Ubiquitin-Proteasome System and Novel Therapeutic Strategies.Cells · 2023Review
- USP37 Deubiquitinates CDC73 in HPT-JT Syndrome.International journal of molecular sciences · 2022Article
- On the Study of Deubiquitinases: Using the Right Tools for the Job.Biomolecules · 2022Review
- Panel of Engineered Ubiquitin Variants Targeting the Family of Human Ubiquitin Interacting Motifs.ACS chemical biology · 2022Article
- Ubiquitin-specific peptidase 37: an important cog in the oncogenic machinery of cancerous cells.Journal of experimental & clinical cancer research : CR · 2021Review
- Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1.The Journal of biological chemistry · 2021Article
- Making Connections: Integrative Signaling Mechanisms Coordinate DNA Break Repair in Chromatin.Frontiers in genetics · 2021Review
- USP37 Promotes Lung Cancer Cell Migration by Stabilizing Snail ProteinFrontiers in genetics · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
USP37 is a deubiquitinase (DUB) with roles in the regulation of DNA damage repair and the cohesion of sister chromatids during mitosis. USP37 contains a unique insert of three ubiquitin interacting motifs (UIMs) within its catalytic DUB domain. We investigated the role of the three UIMs in the ability of USP37 to cleave di-ubiquitin chains. We found that the third UIM of USP37 recognizes the proximal ubiquitin moiety of K48 di-Ub to potentiate cleavage activity and posit that this mechanism of action may be generalizable to other chain types. In the case of K48-linked ubiquitin chains this potentiation stemmed largely from a dramatic increase in catalytic rate (k
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