ArticleThe Journal of biological chemistry2013
Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Noncanonical usage of stop codons in ciliates expands proteins with structurally flexible Q-rich motifs.eLife · 2024Article
- Exploring the "misfolding problem" by systematic discovery and analysis of functional-but-degraded proteins.Molecular biology of the cell · 2023Article
- HSP70-binding motifs function as protein quality control degrons.Cellular and molecular life sciences : CMLS · 2023Article
- Genome-Wide Regulations of the Preinitiation Complex Formation and Elongating RNA Polymerase II by an E3 Ubiquitin Ligase, San1.Molecular and cellular biology · 2022Article
- Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022Review
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites.Biomolecules · 2021Article
- Generalizable Compositional Features Influencing the Proteostatic Fates of Polar Low-Complexity Domains.International journal of molecular sciences · 2021Article
- Deubiquitinases USP20/33 promote the biogenesis of tail-anchored membrane proteins.The Journal of cell biology · 2021Article
- Protein quality control degron-containing substrates are differentially targeted in the cytoplasm and nucleus by ubiquitin ligases.Genetics · 2021Article
- Nuclear Ubiquitin-Proteasome Pathways in Proteostasis Maintenance.Biomolecules · 2021Review
- Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control.Molecular biology of the cell · 2020Article
- Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.Molecular biology of the cell · 2020Article
- Aggregation and degradation scales for prion-like domains: sequence features and context weigh in.Current genetics · 2019Review
- Sequence features governing aggregation or degradation of prion-like proteins.PLoS genetics · 2018Article
- Substrate Insolubility Dictates Hsp104-Dependent Endoplasmic-Reticulum-Associated Degradation.Molecular cell · 2018Article
- Article
- Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.Molecular and cellular biology · 2017Article
- The San1 Ubiquitin Ligase Functions Preferentially with Ubiquitin-conjugating Enzyme Ubc1 during Protein Quality Control.The Journal of biological chemistry · 2016Article
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Authors and funding
4 authors.
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Abstract
Misfolded proteins present an escalating deleterious challenge to cells over the course of their lifetime. One mechanism the cell possesses to prevent misfolded protein accumulation is their destruction by protein quality control (PQC) degradation systems. In eukaryotes, PQC degradation typically proceeds via multiple ubiquitin-protein ligases that act throughout the cell to ubiquitinate misfolded proteins for proteasome degradation. What the exact feature of misfolding that each PQC ubiquitin-protein ligase recognizes in their substrates remains an open question. Our previous studies of the budding yeast nuclear ubiquitin-protein ligase San1 indicated that it recognizes exposed hydrophobicity within its substrates, with the threshold of hydrophobicity equivalent to that of 5 contiguous hydrophobic residues. Here, we uncover an additional parameter: the nature of the exposed hydrophobicity that confers San1-mediated degradation correlates with significant protein insolubility. San1 particularly targets exposed hydrophobicity that leads to insolubility and aggregation above a certain threshold. Our studies presented here provide additional insight into the details of misfolded nuclear protein recognition and demonstrate that there is selectivity for the type of exposed hydrophobicity.
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