ArticleMolecular biology of the cell2013
N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 52 citations in OpenAlex.
- Trichoderma reesei Cellulase in the Monoculture and the Mixed Culture with Aspergillus niger: From Transcripts to Proteins.Applied biochemistry and biotechnology · 2025Article
- Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases.Plant physiology · 2023Article
- Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae.Nature communications · 2023Article
- The ERAD Pathway Participates in Fungal Growth and Cellulase Secretion inJournal of fungi (Basel, Switzerland) · 2023Article
- Up-regulation of ubiquitin-proteasome activity upon loss of NatA-dependent N-terminal acetylation.Life science alliance · 2022Article
- Disruption of the NFrontiers in plant science · 2021Article
- BK channel density is regulated by endoplasmic reticulum associated degradation and influenced by the SKN-1A/NRF1 transcription factor.PLoS genetics · 2020Article
- The Sts1 nuclear import adapter uses a non-canonical bipartite nuclear localization signal and is directly degraded by the proteasome.Journal of cell science · 2020Article
- Regulation of inner nuclear membrane associated protein degradation.Nucleus (Austin, Tex.) · 2019Review
- Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope.Seminars in cell & developmental biology · 2019Review
- N-terminal methionine excision of proteins creates tertiary destabilizing N-degrons of the Arg/N-end rule pathway.The Journal of biological chemistry · 2019Article
- Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases.Molecular cell · 2019Review
- Acetylome in Human Fibroblasts From Parkinson's Disease Patients.Frontiers in cellular neuroscience · 2018Article
- ER-associated degradation regulates Alzheimer's amyloid pathology and memory function by modulating γ-secretase activity.Nature communications · 2017Article
- The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.The Biochemical journal · 2017Review
- Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.Frontiers in plant science · 2017Review
- Article
- A Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.The Journal of biological chemistry · 2016Article
- N-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway.Molecules and cells · 2016Review
- Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms.Scientific reports · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Two conserved ubiquitin ligases, Hrd1 and Doa10, mediate most endoplasmic reticulum-associated protein degradation (ERAD) in yeast. Degradation signals (degrons) recognized by these ubiquitin ligases remain poorly characterized. Doa10 recognizes the Deg1 degron from the MATα2 transcription factor. We previously found that deletion of the gene (NAT3) encoding the catalytic subunit of the NatB N-terminal acetyltransferase weakly stabilized a Deg1-fusion protein. By contrast, a recent analysis of several MATα2 derivatives suggested that N-terminal acetylation of these proteins by NatB was crucial for recognition by Doa10. We now analyze endogenous MATα2 degradation in cells lacking NatB and observe minimal perturbation relative to wild-type cells. However, NatB mutation strongly impairs degradation of ER-luminal Hrd1 substrates. This unexpected defect derives from a failure of Der1, a Hrd1 complex subunit, to be N-terminally acetylated in NatB mutant yeast. We retargeted Der1 to another acetyltransferase to show that it is the only ERAD factor requiring N-terminal acetylation. Preventing Der1 acetylation stimulates its proteolysis via the Hrd1 pathway, at least partially accounting for the ERAD defect observed in the absence of NatB. These results reveal an important role for N-terminal acetylation in controlling Hrd1 ligase activity toward a specific class of ERAD substrates.
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