ReviewCellular logistics
Degradation elements coincide with cofactor binding sites in a short-lived transcription factor.
Review in Cellular logistics. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- UPL5 modulates WHY2 protein distribution in a Kub-site dependent ubiquitination in response to [CaiScience · 2023Article
- Degron masking outlines degronons, co-degrading functional modules in the proteome.Communications biology · 2022Article
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Protein quality control degron-containing substrates are differentially targeted in the cytoplasm and nucleus by ubiquitin ligases.Genetics · 2021Article
- The degradation-promoting roles of deubiquitinases Ubp6 and Ubp3 in cytosolic and ER protein quality control.PloS one · 2020Article
- DNA binding by the MATα2 transcription factor controls its access to alternative ubiquitin-modification pathways.Molecular biology of the cell · 2018Article
- Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elaborate control of gene expression by transcription factors is common to all kingdoms of life. In eukaryotes, transcription factor abundance and activity are often regulated by targeted proteolysis via the ubiquitin-proteasome system (UPS). The yeast MATα2 (α2) cell type regulator has long served as a model for UPS-dependent transcription factor degradation. Proteolysis of α2 is complex: it involves at least 2 ubiquitylation pathways and multiple regions of α2 affect its degradation. Such complexity also exists for the degradation of other UPS substrates. Here I review α2 degradation, most notably our recent identification of 2 novel degradation elements within α2 that overlap corepressor binding sites. I discuss possible implications of these findings and consider how principles of α2 proteolysis may be relevant to the degradation of other UPS substrates.
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Registered trials
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.