Evidence map›Paper›PMID 36459484›Full record

ArticleeLife2022

Modular UBE2H-CTLH E2-E3 complexes regulate erythroid maturation.

Dawafuti Sherpa, Judith Mueller, Özge Karayel, Peng Xu, Yu Yao, Jakub Chrustowicz, Karthik V Gottemukkala, Christine Baumann, Annette Gross, Oliver Czarnecki and 9 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Whole Blood Transcriptomic Analysis of Sickle Cell Trait.European journal of haematology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  9. Article
  10. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Muskelin acts as a substrate receptor of the highly regulatedbioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Identifying E3 Ligase Substrates With Quantitative Degradation Proteomics.Chembiochem : a European journal of chemical biology · 2023
    Article
  20. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    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

19 authors at 3 institutions in 3 countries.

Dawafuti Sherpa *Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Judith Mueller *Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Özge Karayel *Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Peng Xu *Cyrus Tang Medical Institute, National Clinical Research Centre for Hematologic Diseases, Collaborative Innovation Centre of Hematology, State Key Laboratory of Radiation Medicine and Protection, Soochow University, Suzhou, China.ORCID 0000-0002-7573-4813
Yu YaoDepartment of Hematology, St. Jude Children's Research Hospital, Memphis, United States.
Jakub ChrustowiczDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Karthik V GottemukkalaDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Christine BaumannDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Annette GrossDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.
Oliver CzarneckiDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-1767-658X
Wei ZhangDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada.
Jun GuDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada.
Johan NilvebrantDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada.ORCID 0000-0002-6104-6446
Sachdev S SidhuDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada.ORCID 0000-0001-7755-5918
Peter J MurrayDepartment of Immunoregulation, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0001-6329-9802
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0003-1292-4799
Mitchell J WeissDepartment of Hematology, St. Jude Children's Research Hospital, Memphis, United States.ORCID 0000-0003-2460-3036
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-3083-1126
Arno F AlpiDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-9572-7266
Max Planck Institute of Biochemistry · DEUniversity of Toronto · CASt. Jude Children's Research Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of haematopoietic stem cells into mature erythrocytes - erythropoiesis - is a controlled process characterized by cellular reorganization and drastic reshaping of the proteome landscape. Failure of ordered erythropoiesis is associated with anaemias and haematological malignancies. Although the ubiquitin system is a known crucial post-translational regulator in erythropoiesis, how the erythrocyte is reshaped by the ubiquitin system is poorly understood. By measuring the proteomic landscape of in vitro human erythropoiesis models, we found dynamic differential expression of subunits of the CTLH E3 ubiquitin ligase complex that formed maturation stage-dependent assemblies of topologically homologous RANBP9- and RANBP10-CTLH complexes. Moreover, protein abundance of CTLH's cognate E2 ubiquitin conjugating enzyme UBE2H increased during terminal differentiation, and UBE2H expression depended on catalytically active CTLH E3 complexes. CRISPR-Cas9-mediated inactivation of CTLH E3 assemblies or UBE2H in erythroid progenitors revealed defects, including spontaneous and accelerated erythroid maturation as well as inefficient enucleation. Thus, we propose that dynamic maturation stage-specific changes of UBE2H-CTLH E2-E3 modules control the orderly progression of human erythropoiesis.

Indexed as

ErythropoiesisProteomicsErythrocytesGuanine Nucleotide Exchange FactorsHumansMicrotubule-Associated ProteinsProteomeUbiquitinUbiquitin-Conjugating EnzymesGuanine Nucleotide Exchange FactorsMicrotubule-Associated ProteinsProteomeRANBP10 protein, humanUBE2H protein, humanUbiquitinUbiquitin-Conjugating Enzymescell biologyCTLH E3 complexE3 ubiquitin ligaseerythropoiesishumanproteomicsUBE2HUbiquitylation

Identifiers

PMID36459484
PMCPMC9718529
OpenAlexW4311129236

What Socratic holds

Textmetadata
LicenceCC BY
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.