Evidence map›Paper›PMID 24556848›Full record

ArticleMolecular & cellular proteomics : MCP2014

An unbiased proteomic screen reveals caspase cleavage is positively and negatively regulated by substrate phosphorylation.

Jacob P Turowec, Stephanie A Zukowski, James D R Knight, David M Smalley, Lee M Graves, Gary L Johnson, Shawn S C Li, Gilles A Lajoie, David W Litchfield

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Caspase-mediated cleavage events hidden by secondary proteolysis during apoptosis.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. An atlas of caspase cleavage events in differentiating muscle cells.Protein science : a publication of the Protein Society · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Phosphorylation-mediated activation of mouse Xkr8 scramblase for phosphatidylserine exposure.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Caspase 3 cleavage of Pax7 inhibits self-renewal of satellite cells.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. 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

9 authors at 3 institutions in 2 countries.

Jacob P TurowecDepartment of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, Ontario N6A 5C1, Canada;
Stephanie A Zukowski
James D R Knight
David M Smalley
Lee M Graves
Gary L Johnson
Shawn S C Li
Gilles A Lajoie
David W Litchfield
Western University · CAUniversity of North Carolina at Chapel Hill · USLunenfeld-Tanenbaum Research Institute · CA

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
Kinome Reprogramming in Response to Targeted Kinase InhibitorsR01GM101141 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JOHNSON, GARY L. · 2012 to 2015
$1.1M
CIHRNCI NIH HHS CA016086NCI NIH HHS P30 CA016086NIGMS NIH HHS GM101141NIGMS NIH HHS R01 GM101141
6 · The paper itself

Abstract

Post-translational modifications of proteins regulate diverse cellular functions, with mounting evidence suggesting that hierarchical cross-talk between distinct modifications may fine-tune cellular responses. For example, in apoptosis, caspases promote cell death via cleavage of key structural and enzymatic proteins that in some instances is inhibited by phosphorylation near the scissile bond. In this study, we systematically investigated how protein phosphorylation affects susceptibility to caspase cleavage using an N-terminomic strategy, namely, a modified terminal amino isotopic labeling of substrates (TAILS) workflow, to identify proteins for which caspase-catalyzed cleavage is modulated by phosphatase treatment. We validated the effects of phosphorylation on three of the identified proteins and found that Yap1 and Golgin-160 exhibit decreased cleavage when phosphorylated, whereas cleavage of MST3 was promoted by phosphorylation. Furthermore, using synthetic peptides we systematically examined the influence of phosphoserine throughout the entirety of caspase-3, -7, and -8 recognition motifs and observed a general inhibitory effect of phosphorylation even at residues considered outside the classical consensus motif. Overall, our work demonstrates a role for phosphorylation in controlling caspase-mediated cleavage and shows that N-terminomic strategies can be tailored to study cross-talk between phosphorylation and proteolysis.

Indexed as

CaspasesHeLa CellsHippo KinasesHumansIsotope LabelingMembrane ProteinsModels, MolecularPeptidesPhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProteolysisProteomicsCaspasesHippo KinasesMembrane ProteinsPeptidesPhosphoproteinsProtein Serine-Threonine KinasesSTK24 protein, human

Identifiers

PMID24556848
PMCPMC4014278
OpenAlexW2075590318

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.