ArticleProceedings of the National Academy of Sciences of the United States of America2020
Five enzymes of the Arg/N-degron pathway form a targeting complex: The concept of superchanneling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- An Enigma of N-termini dependent protein degradation.Biochemistry and biophysics reports · 2025Article
- Structural basis for the recognition and ubiquitylation of type-2 N-degron substrate by PRT1 plant N-recognin.Nature communications · 2025Article
- Oxygen sensing and plant adaptation to flooding in a changing climate.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Redox regulation: mechanisms, biology and therapeutic targets in diseases.Signal transduction and targeted therapy · 2025Review
- Destined for destruction: The role of methionine aminopeptidases and plant cysteine oxidases in N-degron formation.Plant physiology · 2024Review
- Ubiquitin E3 ligases in the plant Arg/N-degron pathway.The Biochemical journal · 2024Review
- Identification of an Intrinsically Disordered Region (IDR) in Arginyltransferase 1 (ATE1).Biochemistry · 2024Article
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Identification of an intrinsically disordered region (IDR) in arginyltransferase 1 (ATE1).bioRxiv : the preprint server for biology · 2024Article
- Structural study for substrate recognition of human N-terminal glutamine amidohydrolase 1 in the arginine N-degron pathway.Protein science : a publication of the Protein Society · 2024Article
- Arginyltransferase 1 modulates p62-driven autophagy via mTORC1/AMPk signaling.Cell communication and signaling : CCS · 2024Article
- Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies.Molecular cell · 2024Article
- N-Terminal Arginylation Pull-down Analysis Using the R-Catcher Tool.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Variation in ubiquitin system genes creates substrate-specific effects on proteasomal protein degradation.eLife · 2022Article
- Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Arginyl-tRNA-protein transferase 1 (ATE1) promotes melanoma cell growth and migration.FEBS letters · 2022Article
- Structural Characterization of Multienzyme Assemblies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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4 authors at 1 institution in 1 country.
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Abstract
The Arg/N-degron pathway targets proteins for degradation by recognizing their N-terminal (Nt) residues. If a substrate bears, for example, Nt-Asn, its targeting involves deamidation of Nt-Asn, arginylation of resulting Nt-Asp, binding of resulting (conjugated) Nt-Arg to the UBR1-RAD6 E3-E2 ubiquitin ligase, ligase-mediated synthesis of a substrate-linked polyubiquitin chain, its capture by the proteasome, and substrate's degradation. We discovered that the human Nt-Asn-specific Nt-amidase NTAN1, Nt-Gln-specific Nt-amidase NTAQ1, arginyltransferase ATE1, and the ubiquitin ligase UBR1-UBE2A/B (or UBR2-UBE2A/B) form a complex in which NTAN1 Nt-amidase binds to NTAQ1, ATE1, and UBR1/UBR2. In addition, NTAQ1 Nt-amidase and ATE1 arginyltransferase also bind to UBR1/UBR2. In the yeast
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