Evidence map›Paper›PMID 28179995›Full record

ArticleCell death discovery2017

Caspase-mediated proteolysis of the sorting nexin 2 disrupts retromer assembly and potentiates Met/hepatocyte growth factor receptor signaling.

Catherine M Duclos, Audrey Champagne, Julie C Carrier, Caroline Saucier, Christine L Lavoie, Jean-Bernard Denault

Open access · goldAbstract read
In one paragraph

Article in Cell death discovery, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. The emerging role of sorting nexins in cardiovascular diseases.Clinical science (London, England : 1979) · 2019
    Review
  9. Article
  10. Caspases play in traffic.Cell death & disease · 2017
    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

6 authors at 1 institution in 1 country.

Catherine M DuclosDepartment of Pharmacology-Physiology and Institut de Pharmacologie de Sherbrooke, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001, 12th Avenue North, Sherbrooke, QC, Canada J1H 5N4.
Audrey ChampagneDepartment of Anatomy and Cell Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001, 12th Avenue North, Sherbrooke, QC, Canada J1H 5N4.
Julie C CarrierDepartment of Anatomy and Cell Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001, 12th Avenue North, Sherbrooke, QC, Canada J1H 5N4.
Caroline SaucierDepartment of Anatomy and Cell Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001, 12th Avenue North, Sherbrooke, QC, Canada J1H 5N4.ORCID 0000-0001-7678-9886
Christine L LavoieDepartment of Pharmacology-Physiology and Institut de Pharmacologie de Sherbrooke, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001, 12th Avenue North, Sherbrooke, QC, Canada J1H 5N4.
Jean-Bernard DenaultDepartment of Pharmacology-Physiology and Institut de Pharmacologie de Sherbrooke, Faculty of Medicine and Health Sciences, Université de Sherbrooke , 3001, 12th Avenue North, Sherbrooke, QC, Canada J1H 5N4.
Université de Sherbrooke · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolding of apoptosis involves the cleavage of hundreds of proteins by the caspase family of cysteinyl peptidases. Among those substrates are proteins involved in intracellular vesicle trafficking with a net outcome of shutting down the crucial processes governing protein transport to organelles and to the plasma membrane. However, because of the intertwining of receptor trafficking and signaling, cleavage of specific proteins may lead to unintended consequences. Here we show that in apoptosis, sorting nexin 1 and 2 (SNX1 and SNX2), two proteins involved in endosomal sorting, are cleaved by initiator caspases and also by executioner caspase-6 in the case of SNX2. Moreover, SNX1 is cleaved at multiple sites, including following glutamate residues. Cleavage of SNX2 results in a loss of association with the endosome-to-

Identifiers

PMID28179995
PMCPMC5253419
OpenAlexW2582367431

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.