Evidence map›Paper›PMID 19531356›Full record

ArticleDevelopmental cell2009

Metabolic control of oocyte apoptosis mediated by 14-3-3zeta-regulated dephosphorylation of caspase-2.

Leta K Nutt, Marisa R Buchakjian, Eugene Gan, Rashid Darbandi, Sook-Young Yoon, Judy Q Wu, Yuko J Miyamoto, Jennifer A Gibbons, Jennifer A Gibbon, Josh L Andersen and 8 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.3field-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

54 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Cell-Cycle Cross Talk with Caspases and Their Substrates.Cold Spring Harbor perspectives in biology · 2020
    Review
  12. Review
  13. Caspase-2 Substrates: To Apoptosis, Cell Cycle Control, and Beyond.Frontiers in cell and developmental biology · 2020
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Metabolic Regulation of Apoptosis in Cancer.International review of cell and molecular biology · 2016
    Review
  20. Identification of chaperones in a MPPAmerican journal of translational research · 2016
    Article
4 · The record

Corrections and comments

  • Erratum issued
    Gibbon, Jennifer A [corrected to Gibbons, Jennifer A]
5 · Who and what money

Authors and funding

18 authors at 4 institutions in 1 country.

Leta K NuttDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Marisa R Buchakjian
Eugene Gan
Rashid Darbandi
Sook-Young Yoon
Judy Q Wu
Yuko J Miyamoto
Jennifer A Gibbons
Jennifer A Gibbon
Josh L Andersen
Christopher D Freel
Wanli Tang
Changli He
Manabu Kurokawa
Yongjun Wang
Seth S Margolis
Rafael A Fissore
Sally Kornbluth
Duke University · USUniversity of Massachusetts Amherst · USAlbert Einstein College of Medicine · USElon University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007171 · NIGMS · DUKE UNIVERSITY · PI KONTOS, CHRISTOPHER D · 1985 to 2021
$31.2M
Control of caspase activation in apoptosisR01GM080333 · NIGMS · DUKE UNIVERSITY · PI KORNBLUTH, SALLY A · 2007 to 2015
$2.6M
LP3R-1 Regulation and Egg ActivationR01HD051872 · NICHD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI FISSORE, RAFAEL ANTONIO · 2007 to 2011
$1.3M
NICHD NIH HHS HD51872NICHD NIH HHS R01 HD051872NIGMS NIH HHS GM07171NIGMS NIH HHS R01 GM080333NIGMS NIH HHS T32 GM007171
6 · The paper itself

Abstract

Xenopus oocyte death is partly controlled by the apoptotic initiator caspase-2 (C2). We reported previously that oocyte nutrient depletion activates C2 upstream of mitochondrial cytochrome c release. Conversely, nutrient-replete oocytes inhibit C2 via S135 phosphorylation catalyzed by calcium/calmodulin-dependent protein kinase II. We now show that C2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. Moreover, we determined that S135 dephosphorylation is catalyzed by protein phosphatase-1 (PP1), which directly binds C2. Although C2 dephosphorylation is responsive to metabolism, neither PP1 activity nor binding is metabolically regulated. Rather, release of 14-3-3zeta from C2 is controlled by metabolism and allows for C2 dephosphorylation. Accordingly, a C2 mutant unable to bind 14-3-3zeta is highly susceptible to dephosphorylation. Although this mechanism was initially established in Xenopus, we now demonstrate similar control of murine C2 by phosphorylation and 14-3-3 binding in mouse eggs. These findings provide an unexpected evolutionary link between 14-3-3 and metabolism in oocyte death.

Indexed as

Apoptosis14-3-3 ProteinsAnimalsCaspase 2Enzyme ActivationFemaleMiceOocytesPhosphorylationProtein BindingProtein Phosphatase 1Xenopus14-3-3 ProteinsCaspase 2Protein Phosphatase 1

Identifiers

PMID19531356
PMCPMC2698816
OpenAlexW2091501983

What OpenQuestion holds

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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.