Evidence map›Paper›PMID 27601470›Full record

ArticleThe Journal of biological chemistry2016

Phosphorylation Impacts N-end Rule Degradation of the Proteolytically Activated Form of BMX Kinase.

Mohamed A Eldeeb, Richard P Fahlman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Targeting the BMX in cancer: molecular mechanisms and emerging therapeutic strategies.Journal of enzyme inhibition and medicinal chemistry · 2026
    Review
  2. An Enigma of N-termini dependent protein degradation.Biochemistry and biophysics reports · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Signaling Pathways Regulated by UBR Box-Containing E3 Ligases.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Degradation of proteins with N-terminal glycine.Nature structural & molecular biology · 2019
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Mohamed A EldeebFrom the Departments of Biochemistry and.
Richard P FahlmanFrom the Departments of Biochemistry and rfahlman@ualberta.ca.
University of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular signaling leading to the initiation of apoptosis typically results in the activation of caspases, which in turn leads to the proteolytic generation of protein fragments with new or altered cellular functions. Increasing numbers of reports are demonstrating that the activity of many of these proteolytically activated protein fragments can be attenuated by their selective degradation by the N-end rule pathway. Here we report the first evidence that selective degradation of a caspase product by the N-end rule pathway can be modulated by phosphorylation. We demonstrate that the pro-apoptotic fragment of the bone marrow kinase on chromosome X (BMX) generated by caspase cleavage in the prostate cancer-derived PC3 cell line is metabolically unstable in cells because its N-terminal tryptophan targets it for proteasomal degradation via the N-end rule pathway. In addition, we have demonstrated that phosphorylation of tyrosine 566 relatively inhibits degradation of the C-terminal BMX catalytic fragment, and this phosphorylation is crucial for its pro-apoptotic function. Overall, our results demonstrate that cleaved BMX is a novel N-end rule substrate, and its degradation exhibits a novel interplay between substrate phosphorylation and N-end rule degradation, revealing an increasing complex regulatory network of apoptotic proteolytic signaling cascades.

Indexed as

ProteolysisApoptosisCell Line, TumorHumansPhosphorylationProtein-Tyrosine KinasesSignal TransductionBMX protein, humanProtein-Tyrosine KinasesapoptosisBMXEtkN-end Rulephosphorylationprotein degradationtyrosine-protein kinase (tyrosine kinase)ubiquitin ligase

Identifiers

PMID27601470
PMCPMC5077209
OpenAlexW2513482984

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.