Evidence map›Paper›PMID 37844242›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Molecular basis for C-degron recognition by CRL2

Shidong Zhao, Diana Olmayev-Yaakobov, Wenwen Ru, Shanshan Li, Xinyan Chen, Jiahai Zhang, Xuebiao Yao, Itay Koren, Kaiming Zhang, Chao Xu

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  10. Article
  11. Review
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Shidong Zhao *Ministry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Diana Olmayev-Yaakobov *The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 5290002, Israel.ORCID 0000-0002-8168-2116
Wenwen RuMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Shanshan LiMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Xinyan ChenMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Jiahai ZhangMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Xuebiao YaoMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Itay KorenThe Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 5290002, Israel.ORCID 0000-0002-5693-1651
Kaiming ZhangMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.
Chao XuMinistry of Education Key Laboratory for Cellular Dynamics, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Peoples Republic of China.ORCID 0000-0003-0444-7080
University of Science and Technology of China · CNBar-Ilan University · IL

Funding

European Research Council 947709
6 · The paper itself

Abstract

E3 ubiquitin ligases determine the specificity of eukaryotic protein degradation by selective binding to destabilizing protein motifs, termed degrons, in substrates for ubiquitin-mediated proteolysis. The exposed C-terminal residues of proteins can act as C-degrons that are recognized by distinct substrate receptors (SRs) as part of dedicated cullin-RING E3 ubiquitin ligase (CRL) complexes. APPBP2, an SR of Cullin 2-RING ligase (CRL2), has been shown to recognize R-x-x-G/C-degron; however, the molecular mechanism of recognition remains elusive. By solving several cryogenic electron microscopy structures of active CRL2

Indexed as

Cullin ProteinsUbiquitinAmino Acid MotifsProteolysisUbiquitin-Protein LigasesCullin ProteinsUbiquitinUbiquitin-Protein LigasesC-degronCryo-EMCullin-RING E3 ubiquitin ligaseprotein degradationUbiquitin-proteasome system

Identifiers

PMID37844242
PMCPMC10614623
OpenAlexW4387665074

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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 Socratic graph.