ReviewBiomolecules2014
Proteins directly interacting with mammalian 20S proteasomal subunits and ubiquitin-independent proteasomal degradation.
Review in Biomolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Mechanisms of ubiquitin-independent proteasomal degradation and their roles in age-related neurodegenerative disease.Frontiers in cell and developmental biology · 2024Review
- Acceleration of Protein Degradation by 20S Proteasome-Binding Peptides Generated by In Vitro Artificial Evolution.International journal of molecular sciences · 2023Article
- Widespread intron retention impairs protein homeostasis in C9orf72 ALS brains.Genome research · 2020Article
- Degron capability of the hydrophobic C-terminus of the polyglutamine disease protein, ataxin-3.Journal of neuroscience research · 2020Article
- Thymoproteasome-Expressing Mesenchymal Stromal Cells Confer Protective Anti-Tumor ImmunityFrontiers in immunology · 2020Article
- CSN6 promotes tumorigenesis of gastric cancer by ubiquitin-independent proteasomal degradation of p16Cancer biology & medicine · 2019Article
- Chemokine signaling links cell-cycle progression and cilia formation for left-right symmetry breaking.PLoS biology · 2019Article
- The PSMA8 subunit of the spermatoproteasome is essential for proper meiotic exit and mouse fertility.PLoS genetics · 2019Article
- Proline- and Arginine-Rich Peptides as Flexible Allosteric Modulators of Human Proteasome Activity.Journal of medicinal chemistry · 2019Article
- Lysine-Less Variants of Spinal Muscular Atrophy SMN and SMNΔ7 Proteins Are Degraded by the Proteasome Pathway.International journal of molecular sciences · 2017Article
- The ER retention protein RER1 promotes alpha-synuclein degradation via the proteasome.PloS one · 2017Article
- Phosphorylation of the C-terminal tail of proteasome subunit α7 is required for binding of the proteasome quality control factor Ecm29.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The mammalian 20S proteasome is a heterodimeric cylindrical complex (α7β7β7α7), composed of four rings each composed of seven different α or β subunits with broad proteolytic activity. We review the mammalian proteins shown to directly interact with specific 20S proteasomal subunits and those subjected to ubiquitin-independent proteasomal degradation (UIPD). The published reports of proteins that interact with specific proteasomal subunits, and others found on interactome databases and those that are degraded by a UIPD mechanism, overlap by only a few protein members. Therefore, systematic studies of the specificity of the interactions, the elucidation of the protein regions implicated in the interactions (that may or may not be followed by degradation) and competition experiments between proteins known to interact with the same proteasomal subunit, are needed. Those studies should provide a coherent picture of the molecular mechanisms governing the interactions of cellular proteins with proteasomal subunits, and their relevance to cell proteostasis and cell functioning.
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