ArticleNature communications2022
CRL2
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular insights into NLRP1 Gly/N-degron recognition by CRL2Acta crystallographica. Section F, Structural biology communications · 2026Article
- Structure of the E3 ligase CRL2Cell reports · 2026Article
- Structures of ZYG11B-EloB-EloC-substrate complex reveal mechanisms of CRL2Nature communications · 2026Article
- CUL4A-DDB1-DCAF10 is an N-recognin for N-terminally acetylated Src kinases.Nature communications · 2026Article
- Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025Review
- Reduced Pressure Ionization Enhances Native Mass Spectrometry of Proteins and Protein Complexes.Angewandte Chemie (International ed. in English) · 2025Article
- The generation and consequences of N-terminal proteoform diversity.Cell reports · 2025Review
- Global profiling of N-terminal cysteine-dependent degradation mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Linker-free PROTACs efficiently induce the degradation of oncoproteins.Nature communications · 2025Article
- Identification of a non-inhibitory aptameric ligand to CRL2Nature communications · 2025Article
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Structural basis for C-degron selectivity across KLHDCX family E3 ubiquitin ligases.Nature communications · 2024Article
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- SARS-CoV-2 ORF10 hijacking ubiquitination machinery reveals potential unique drug targeting sites.Acta pharmaceutica Sinica. B · 2024Article
- Molecular insights into degron recognition by CRL5Nature communications · 2024Article
- 1-L Transcription of SARS-CoV-2 Spike Protein S1 Subunit.International journal of molecular sciences · 2024Article
- N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.Nature communications · 2023Article
- NatB Catalytic Subunit Depletion Disrupts DNA Replication Initiation Leading to Senescence in MEFs.International journal of molecular sciences · 2023Article
- Recognition of an Ala-rich C-degron by the E3 ligase Pirh2.Nature communications · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
N-degron pathway plays an important role in the protein quality control and maintenance of cellular protein homeostasis. ZER1 and ZYG11B, the substrate receptors of the Cullin 2-RING E3 ubiquitin ligase (CRL2), recognize N-terminal (Nt) glycine degrons and participate in the Nt-myristoylation quality control through the Gly/N-degron pathway. Here we show that ZER1 and ZYG11B can also recognize small Nt-residues other than glycine. Specifically, ZER1 binds better to Nt-Ser, -Ala, -Thr and -Cys than to -Gly, while ZYG11B prefers Nt-Gly but also has the capacity to recognize Nt-Ser, -Ala and -Cys in vitro. We found that Nt-Ser, -Ala and -Cys undergo Nt-acetylation catalyzed by Nt-acetyltransferase (NAT), thereby shielding them from recognition by ZER1/ZYG11B in cells. Instead, ZER1/ZYG11B readily targets a selection of small Nt-residues lacking Nt-acetylation for degradation in NAT-deficient cells, implicating its role in the Nt-acetylation quality control. Furthermore, we present the crystal structures of ZER1 and ZYG11B bound to various small Nt-residues and uncover the molecular mechanism of non-acetylated substrate recognition by ZER1 and ZYG11B.
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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.