Evidence map›Paper›PMID 28082348›Full record

ArticleMolecular systems biology2017

Interactome disassembly during apoptosis occurs independent of caspase cleavage.

Nichollas E Scott, Lindsay D Rogers, Anna Prudova, Nat F Brown, Nikolaus Fortelny, Christopher M Overall, Leonard J Foster

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 2 pooled it
4.1field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 2 syntheses or guidelines pooled it, 59 citations in OpenAlex.

  1. Pooled it
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  20. Biogenesis of the SpaciousInfection and immunity · 2020
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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

7 authors at 1 institution in 1 country.

Nichollas E ScottMichael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Lindsay D RogersDepartment of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, BC, Canada.
Anna PrudovaMichael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Nat F BrownMichael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Nikolaus FortelnyMichael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Christopher M OverallDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada.
Leonard J FosterMichael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada foster@chibi.ubc.ca.ORCID 0000-0001-8551-4817
University of British Columbia · CA

Funding

CIHR MOP‐77688
6 · The paper itself

Abstract

Protein-protein interaction networks (interactomes) define the functionality of all biological systems. In apoptosis, proteolysis by caspases is thought to initiate disassembly of protein complexes and cell death. Here we used a quantitative proteomics approach, protein correlation profiling (PCP), to explore changes in cytoplasmic and mitochondrial interactomes in response to apoptosis initiation as a function of caspase activity. We measured the response to initiation of Fas-mediated apoptosis in 17,991 interactions among 2,779 proteins, comprising the largest dynamic interactome to date. The majority of interactions were unaffected early in apoptosis, but multiple complexes containing known caspase targets were disassembled. Nonetheless, proteome-wide analysis of proteolytic processing by terminal amine isotopic labeling of substrates (TAILS) revealed little correlation between proteolytic and interactome changes. Our findings show that, in apoptosis, significant interactome alterations occur before and independently of caspase activity. Thus, apoptosis initiation includes a tight program of interactome rearrangement, leading to disassembly of relatively few, select complexes. These early interactome alterations occur independently of cleavage of these protein by caspases.

Indexed as

ApoptosisCaspasesChromatography, LiquidCytoplasmfas ReceptorHumansIsotope LabelingJurkat CellsMass SpectrometryMitochondriaProtein Interaction MapsProteolysisProteomicsCaspasesFAS protein, humanfas Receptorcaspaseprotein complexesprotein correlation profilingSILAC

Identifiers

PMID28082348
PMCPMC5293159
OpenAlexW2576030387

What OpenQuestion 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 OpenQuestion graph.