Evidence map›Paper›PMID 33636084›Full record

ArticleBiochemistry2021

SPIN4 Is a Principal Endogenous Substrate of the E3 Ubiquitin Ligase DCAF16.

Xiaoyu Zhang, Marvin Thielert, Haoxin Li, Benjamin F Cravatt

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Covalent Reprogramming of Kinase Binders to Modulate Protein Abundance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Covalent Reprogramming of Kinase Binders to Modulate Protein Homeostasis.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Identifying E3 Ligase Substrates With Quantitative Degradation Proteomics.Chembiochem : a European journal of chemical biology · 2023
    Article
  13. Review
  14. 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

4 authors at 1 institution in 1 country.

Xiaoyu ZhangDepartment of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92307, United States.ORCID 0000-0002-0951-9664
Marvin ThielertDepartment of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92307, United States.
Haoxin LiDepartment of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92307, United States.
Benjamin F CravattDepartment of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92307, United States.ORCID 0000-0001-5330-3492
Scripps Research Institute · US

Funding

Chemical Proteomic Platforms for Radically Expanding Cancer DruggabilityR35CA231991 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI BENJAMIN F CRAVATT · 2018 to 2026
$9.5M
Discovery of small molecule-mediated protein degradation pathways in human cancerK99CA248715 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI ZHANG, XIAOYU · 2020 to 2021
$247k
NCI NIH HHS K99 CA248715NCI NIH HHS R35 CA231991
6 · The paper itself

Abstract

DCAF16 is a substrate recognition component of Cullin-RING E3 ubiquitin ligases that can be targeted by electrophilic PROTACs (proteolysis targeting chimeras) to promote the nuclear-restricted degradation of proteins. The endogenous protein substates of DCAF16 remain unknown. In this study, we compared the protein content of DCAF16-wild type and DCAF16-knockout (KO) cells by untargeted mass spectrometry-based proteomics, identifying the Tudor domain-containing protein Spindlin-4 (SPIN4) as a protein with a level that was substantially increased in cells lacking DCAF16. Very few other proteomic changes were found in DCAF16-KO cells, pointing to a specific relationship between DCAF16 and SPIN4. Consistent with this hypothesis, we found that DCAF16 interacts with and ubiquitinates SPIN4, but not other related SPIN proteins, and identified a conserved lysine residue unique to SPIN4 that is involved in DCAF16 binding. Finally, we provide evidence that SPIN4 preferentially binds trimethylated histone H3K4 over other modified histone modifications. These results, taken together, indicate that DCAF16 and SPIN4 form a dedicated E3 ligase-substrate complex that regulates the turnover and presumed functions of SPIN4 in human cells.

Indexed as

Protein Processing, Post-TranslationalUbiquitinationCell Cycle ProteinsHEK293 CellsHumansMicrotubule-Associated ProteinsPhosphoproteinsProteolysisSubstrate SpecificityUbiquitinUbiquitin-Protein LigasesCell Cycle ProteinsMicrotubule-Associated ProteinsPhosphoproteinsspindlinUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID33636084
PMCPMC8325951
OpenAlexW3129243832

What OpenQuestion holds

Textmetadata
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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.