Evidence map›Paper›PMID 37166757›Full record

ArticleChembiochem : a European journal of chemical biology2023

Identifying E3 Ligase Substrates With Quantitative Degradation Proteomics.

Victoria N Jordan, Alban Ordureau, Heeseon An

Open access · bronzeAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
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

3 authors at 1 institution in 1 country.

Victoria N JordanChemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.ORCID 0000-0001-6310-8244
Alban OrdureauCell Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.ORCID 0000-0002-4924-8520
Heeseon AnChemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.ORCID 0000-0002-8518-4077
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
Tri-Institutional PhD Program in Chemical BiologyT32GM136640 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI DEREK S TAN · 2020 to 2026
$2.4M
NCI NIH HHS P30 CA008748NIGMS NIH HHS T32 GM136640
6 · The paper itself

Abstract

Controlled protein degradation by the ubiquitin-proteasome pathway is critical for almost all cellular processes. E3 ubiquitin ligases are responsible for targeting proteins for ubiquitylation and subsequent proteasomal degradation with spatial and temporal precision. While studies have revealed various E3-substrate pairs involved in distinct biological processes, the complete substrate profiles of individual E3 ligases are largely unknown. Here we report a new approach to identify substrates of an E3 ligase for proteasomal degradation using unnatural amino acid incorporation pulse-chase proteomics (degradomics). Applying this approach, we determine the steady-state substrates of the C-terminal to LisH (CTLH) E3 ligase, a multi-component complex with poorly defined substrates. By comparing the proteome degradation profiles of active and inactive CTLH-expressing cells, we successfully identify previously known and new potential substrates of CTLH ligase. Altogether, degradomics can comprehensively identify degradation substrates of an E3 ligase, which can be adapted for other E3 ligases in various cellular contexts.

Indexed as

ProteomicsUbiquitin-Protein LigasesProteolysisUbiquitinationUbiquitinsUbiquitin-Protein LigasesUbiquitinsCTLHDegradomicsProtein half-lifeThe Ubiquitin Proteasome SystemUbiquitin

Identifiers

PMID37166757
PMCPMC10548883
OpenAlexW4376133051

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.