Evidence map›Paper›PMID 27723735›Full record

ArticleNature structural & molecular biology2016

Regulation of CED-3 caspase localization and activation by C. elegans nuclear-membrane protein NPP-14.

Xudong Chen, Yue Wang, Yu-Zen Chen, Brian L Harry, Akihisa Nakagawa, Eui-Seung Lee, Hongyan Guo, Ding Xue

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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

8 authors at 2 institutions in 2 countries.

Xudong ChenSchool of Life Sciences, Tsinghua University, Beijing, China.
Yue WangSchool of Life Sciences, Tsinghua University, Beijing, China.
Yu-Zen ChenDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, Colorado, USA.
Brian L HarryDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, Colorado, USA.
Akihisa NakagawaDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, Colorado, USA.
Eui-Seung LeeDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, Colorado, USA.
Hongyan GuoSchool of Life Sciences, Tsinghua University, Beijing, China.
Ding XueSchool of Life Sciences, Tsinghua University, Beijing, China.
Tsinghua University · CNUniversity of Colorado Boulder · US

Funding

Medical Scientist Training ProgramT32GM008497 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI WILSON, CARA C. · 1993 to 2022
$15.2M
Fundamental mechanisms of paternal mitochondrial eliminationand radiation-induced bystander effectsR35GM118188 · NIGMS · UNIVERSITY OF COLORADO · PI DING XUE · 2016 to 2026
$6.8M
MOLECULAR BIOLOGYT32GM007135 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI KRAUTER, KENNETH S · 1985 to 2012
$5.7M
TARGETS OF THE CELL DEATH PROTEASESR01GM059083 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI XUE, DING · 1999 to 2012
$3.7M
Regulation of Cell Death ActivationR01GM088241 · NIGMS · UNIVERSITY OF COLORADO · PI XUE, DING · 2010 to 2013
$1.1M
Execution of apoptosis in C. elegans mediated by ubiquilin homologue cps-4 and prF30NS070596 · NINDS · UNIVERSITY OF COLORADO · PI HARRY, BRIAN · 2010 to 2012
$70k
NIGMS NIH HHS R01 GM059083NIGMS NIH HHS R01 GM088241NIGMS NIH HHS R35 GM118188NIGMS NIH HHS T32 GM007135NIGMS NIH HHS T32 GM008497NINDS NIH HHS F30 NS070596
6 · The paper itself

Abstract

Caspases are cysteine proteases with critical roles in apoptosis. The Caenorhabditis elegans caspase CED-3 is activated by autocatalytic cleavage, a process enhanced by CED-4. Here we report that the CED-3 zymogen localizes to the perinuclear region in C. elegans germ cells and that CED-3 autocatalytic cleavage is held in check by C. elegans nuclei and activated by CED-4. The nuclear-pore protein NPP-14 interacts with the CED-3 zymogen prodomain, colocalizes with CED-3 in vivo and inhibits CED-3 autoactivation in vitro. Several missense mutations in the CED-3 prodomain result in stronger association with NPP-14 and decreased CED-3 activation by CED-4 in the presence of nuclei or NPP-14, thus leading to cell-death defects. Those same mutations enhance autocatalytic cleavage of CED-3 in vitro and increase apoptosis in vivo in the absence of npp-14. Our results reveal a critical role of nuclei and nuclear-membrane proteins in regulating the activation and localization of CED-3.

Indexed as

ApoptosisAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCaspasesEnzyme ActivationGerm CellsMutation, MissenseNuclear Pore Complex ProteinsProtein Interaction Domains and MotifsCaenorhabditis elegans ProteinsCaspasesced-3 protein, C elegansNPP-14 protein, C elegansNuclear Pore Complex Proteins

Identifiers

PMID27723735
PMCPMC5484413
OpenAlexW2530630892

What OpenQuestion holds

Textmetadata
LicenceTDM
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.