ArticleProceedings of the National Academy of Sciences of the United States of America2008
Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- A machine learning model predicts protein stability of annotated and alternate protein isoforms.bioRxiv : the preprint server for biology · 2026Article
- 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
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- Article
- 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
- Up-regulation of ubiquitin-proteasome activity upon loss of NatA-dependent N-terminal acetylation.Life science alliance · 2022Article
- Ubr1-mediated ubiquitylation orchestrates asexual development, polar growth, and virulence-related cellular events in Beauveria bassiana.Applied microbiology and biotechnology · 2021Article
- Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.The Journal of biological chemistry · 2016Article
- Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway.The Journal of biological chemistry · 2016Article
- Functional implications and ubiquitin-dependent degradation of the peptide transporter Ptr2 in Saccharomyces cerevisiae.Eukaryotic cell · 2014Article
- Profiling human protein degradome delineates cellular responses to proteasomal inhibition and reveals a feedback mechanism in regulating proteasome homeostasis.Cell research · 2014Article
- Analysing the substrate multispecificity of a proton-coupled oligopeptide transporter using a dipeptide library.Nature communications · 2013Article
- The Mck1 GSK-3 kinase inhibits the activity of Clb2-Cdk1 post-nuclear division.Cell cycle (Georgetown, Tex.) · 2012Article
- Regulation of amino acid, nucleotide, and phosphate metabolism in Saccharomyces cerevisiae.Genetics · 2012Article
- The N-end rule pathway.Annual review of biochemistry · 2012Review
- The N-end rule pathway and regulation by proteolysis.Protein science : a publication of the Protein Society · 2011Review
- Ubiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndrome.PloS one · 2011Article
- The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases.Nature cell biology · 2010Article
- Protein aggregation induced during glass bead lysis of yeast.Yeast (Chichester, England) · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Substrates of the N-end rule pathway include proteins with destabilizing N-terminal residues. These residues are recognized by E3 ubiquitin ligases called N-recognins. Ubr1 is the N-recognin of the yeast Saccharomyces cerevisiae. Extracellular amino acids or short peptides up-regulate the peptide transporter gene PTR2, thereby increasing the capacity of a cell to import peptides. Cup9 is a transcriptional repressor that down-regulates PTR2. The induction of PTR2 by peptides or amino acids involves accelerated degradation of Cup9 by the N-end rule pathway. We report here that the Ubr1 N-recognin, which conditionally targets Cup9 for degradation, is phosphorylated in vivo at multiple sites, including Ser(300) and Tyr(277). We also show that the type-I casein kinases Yck1 and Yck2 phosphorylate Ubr1 on Ser(300), and thereby make possible ("prime") the subsequent (presumably sequential) phosphorylations of Ubr1 on Ser(296), Ser(292), Thr(288), and Tyr(277) by Mck1, a kinase of the glycogen synthase kinase 3 (Gsk3) family. Phosphorylation of Ubr1 on Tyr(277) by Mck1 is a previously undescribed example of a cascade-based tyrosine phosphorylation by a Gsk3-type kinase outside of autophosphorylation. We show that the Yck1/Yck2-mediated phosphorylation of Ubr1 on Ser(300) plays a major role in the control of peptide import by the N-end rule pathway. In contrast to phosphorylation on Ser(300), the subsequent (primed) phosphorylations, including the one on Tyr(277), have at most minor effects on the known properties of Ubr1, including regulation of peptide import. Thus, a biological role of the rest of Ubr1 phosphorylation cascade remains to be identified.
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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.