Evidence map›Paper›PMID 25853217›Full record

ArticleCell cycle (Georgetown, Tex.)2015

Human ACAP2 is a homolog of C. elegans CNT-1 that promotes apoptosis in cancer cells.

Kelly D Sullivan, Akihisa Nakagawa, Ding Xue, Joaquín M Espinosa

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
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  6. A novel lncRNA-mRNA-miRNA signature predicts recurrence and disease-free survival in cervical cancer.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2021
    Article
  7. 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

4 authors at 2 institutions in 1 country.

Kelly D Sullivana Department of Molecular, Cellular, and Developmental Biology; University of Colorado ; Boulder , CO , USA.
Akihisa Nakagawa
Ding Xue
Joaquín M Espinosa
University of Colorado System · USUniversity of Colorado Boulder · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Stress- and Promoter-Specific Mechanisms of Transcritpional Activation by p53R01CA117907 · NCI · UNIVERSITY OF COLORADO DENVER · PI ESPINOSA, JOAQUIN M. · 2006 to 2022
$4.4M
TARGETS OF THE CELL DEATH PROTEASESR01GM059083 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI XUE, DING · 1999 to 2012
$3.7M
Chromatin Degradation During ApoptosisR01GM079097 · NIGMS · UNIVERSITY OF COLORADO · PI XUE, DING · 2007 to 2015
$2.3M
NCI NIH HHS P30 CA046934NCI NIH HHS R01 CA117907NCI NIH HHS R01CA117907NIGMS NIH HHS R01GM059083NIGMS NIH HHS R01GM079097
6 · The paper itself

Abstract

Activation of caspases is an integral part of the apoptotic cell death program. Collectively, these proteases target hundreds of substrates, leading to the hypothesis that apoptosis is "death by a thousand cuts". Recent work, however, has demonstrated that caspase cleavage of only a subset of these substrates directs apoptosis in the cell. One such example is C. elegans CNT-1, which is cleaved by CED-3 to generate a truncated form, tCNT-1, that acquires a potent phosphoinositide-binding activity and translocates to the plasma membrane where it inactivates AKT survival signaling. We report here that ACAP2, a homolog of C. elegans CNT-1, has a pro-apoptotic function and an identical phosphoinositide-binding pattern to that of tCNT-1, despite not being an apparent target of caspase cleavage. We show that knockdown of ACAP2 blocks apoptosis in cancer cells in response to the chemotherapeutic antimetabolite 5-fluorouracil and that ACAP2 expression is down-regulated in some esophageal cancers, leukemias and lymphomas. These results suggest that ACAP2 is a functional homolog of C. elegans CNT-1 and its inactivation or downregulation in human cells may contribute to cancer development.

Indexed as

ApoptosisAmino Acid SequenceAnimalsCaenorhabditis elegans ProteinsCaspasesCell Line, TumorDown-RegulationEnzyme ActivationFluorouracilGene Expression ProfilingGene Expression RegulationGTPase-Activating ProteinsHCT116 CellsHumansLigandsLipidsACAP1 protein, humanACAP2 protein, humanCaenorhabditis elegans ProteinsCaspasesCNT-1 protein, C elegansFluorouracilGTPase-Activating ProteinsLigandsLipidsMembrane ProteinsProto-Oncogene Proteins c-akt

Identifiers

PMID25853217
PMCPMC4614986
OpenAlexW1736264649

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.