Evidence map›Paper›PMID 17880263›Full record

ArticlePLoS biology2007

A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila.

Eli Arama, Maya Bader, Gabrielle E Rieckhof, Hermann Steller

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

81 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. CRL2BMC biology · 2025
    Article
  6. Reduction in Gonad Development and Sperm Motility in Male Brown PlanthopperInternational journal of molecular sciences · 2025
    Article
  7. hLife · 2025
    Article
  8. Article
  9. Genome-Wide Identification and Expression Analysis of theInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Cells · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Non-Canonical Roles of Apoptotic Caspases in the Nervous System.Frontiers in cell and developmental biology · 2022
    Review
  20. The roles of KLHL family members in human cancers.American journal of cancer research · 2022
    Review

21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Eli AramaStrang Laboratory of Cancer Research, The Rockefeller University, New York, New York, United States of America.
Maya Bader
Gabrielle E Rieckhof
Hermann Steller
Rockefeller University · USHoward Hughes Medical Institute · US

Funding

Proteasome Regulation and Function in Cellular RemodelingR01GM060124 · NIGMS · ROCKEFELLER UNIVERSITY · PI STELLER, HERMANN · 1999 to 2018
$5.4M
NIGMS NIH HHS R01 GM060124NIGMS NIH HHS R01 GM60124
6 · The paper itself

Abstract

In both insects and mammals, spermatids eliminate their bulk cytoplasm as they undergo terminal differentiation. In Drosophila, this process of dramatic cellular remodeling requires apoptotic proteins, including caspases. To gain further insight into the regulation of caspases, we screened a large collection of sterile male flies for mutants that block effector caspase activation at the onset of spermatid individualization. Here, we describe the identification and characterization of a testis-specific, Cullin-3-dependent ubiquitin ligase complex that is required for caspase activation in spermatids. Mutations in either a testis-specific isoform of Cullin-3 (Cul3(Testis)), the small RING protein Roc1b, or a Drosophila orthologue of the mammalian BTB-Kelch protein Klhl10 all reduce or eliminate effector caspase activation in spermatids. Importantly, all three genes encode proteins that can physically interact to form a ubiquitin ligase complex. Roc1b binds to the catalytic core of Cullin-3, and Klhl10 binds specifically to a unique testis-specific N-terminal Cullin-3 (TeNC) domain of Cul3(Testis) that is required for activation of effector caspase in spermatids. Finally, the BIR domain region of the giant inhibitor of apoptosis-like protein dBruce is sufficient to bind to Klhl10, which is consistent with the idea that dBruce is a substrate for the Cullin-3-based E3-ligase complex. These findings reveal a novel role of Cullin-based ubiquitin ligases in caspase regulation.

Indexed as

Amino Acid SequenceAnimalsCaspasesCell Cycle ProteinsCell DifferentiationCullin ProteinsDrosophila melanogasterDrosophila ProteinsEnzyme ActivationFemaleGene Expression Regulation, EnzymologicMaleMolecular Sequence DataMutationSpermatogenesisSpermatozoaCaspasesCell Cycle ProteinsCul3 protein, DrosophilaCullin ProteinsDrosophila Proteins

Identifiers

PMID17880263
PMCPMC1976628
OpenAlexW2126032058

What OpenQuestion holds

Textmetadata
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.