ArticleJournal of molecular biology2007
Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating enzyme.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Deubiquitinase Ubp3 regulates ribophagy and deubiquitinates Smo1 for appressorium-mediated infection by Magnaporthe oryzae.Molecular plant pathology · 2022Article
- SARS-CoV-2 Nucleocapsid Protein Targets a Conserved Surface Groove of the NTF2-like Domain of G3BP1.Journal of molecular biology · 2022Article
- Ribosomal protein S7 ubiquitination during ER stress in yeast is associated with selective mRNA translation and stress outcome.Scientific reports · 2020Article
- Deubiquitination and the regulation of stress granule assembly.Current genetics · 2016Review
- The Catalytic Activity of the Ubp3 Deubiquitinating Protease Is Required for Efficient Stress Granule Assembly in Saccharomyces cerevisiae.Molecular and cellular biology · 2016Article
- Both the autophagy and proteasomal pathways facilitate the Ubp3p-dependent depletion of a subset of translation and RNA turnover factors during nitrogen starvation in Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2015Article
- Ubiquitylation by the Ltn1 E3 ligase protects 60S ribosomes from starvation-induced selective autophagy.The Journal of cell biology · 2014Article
- The ubiquitin-proteasome system of Saccharomyces cerevisiae.Genetics · 2012Review
- Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress.The EMBO journal · 2011Article
- Proteome-wide search reveals unexpected RNA-binding proteins in Saccharomyces cerevisiae.PloS one · 2010Article
- Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy.EMBO reports · 2010Article
- Protein partners of deubiquitinating enzymes.The Biochemical journal · 2008Review
- Deubiquitinase Ubp3 enhances the proteasomal degradation of key enzymes in sterol homeostasis.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
5 authors at 5 institutions in 2 countries.
Funding
Abstract
Yeast Ubp3 and its co-factor Bre5 form a deubiquitylation complex to regulate protein transport between the endoplasmic reticulum and Golgi compartments of the cell. A novel N-terminal domain of the Ubp3 catalytic subunit forms a complex with the NTF2-like domain of the Bre5 regulatory subunit. Here, we report the X-ray crystal structure of an Ubp3-Bre5 complex and show that it forms a symmetric hetero-tetrameric complex in which the Bre5 NTF2-like domain dimer interacts with two L-shaped beta-strand-turn-alpha-helix motifs of Ubp3. The Ubp3 N-terminal domain binds within a hydrophobic cavity on the surface of the Bre5 NTF2-like domain subunit with conserved residues within both proteins interacting predominantly through antiparallel beta-sheet hydrogen bonds and van der Waals contacts. Structure-based mutagenesis and functional studies confirm the significance of the observed interactions for Ubp3-Bre5 association in vitro and Ubp3 function in vivo. Comparison of the structure to other protein complexes with NTF2-like domains shows that the Ubp3-Bre5 interface is novel. Together, these studies provide new insights into Ubp3 recognition by Bre5 and into protein recognition by NTF2-like domains.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.