Evidence map›Paper›PMID 16642037›Full record

ArticleThe EMBO journal2006

Nuclear Akt associates with PKC-phosphorylated Ebp1, preventing DNA fragmentation by inhibition of caspase-activated DNase.

Jee-Yin Ahn, Xia Liu, Zhixue Liu, Lorena Pereira, Dongmei Cheng, Junmin Peng, Paul A Wade, Anne W Hamburger, Keqiang Ye

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
  2. ITAFProceedings of the National Academy of Sciences of the United States of America · 2025
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  8. Roles of ErbB3-binding protein 1 (EBP1) in embryonic development and gene-silencing control.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  20. Overexpression of aFrontiers in plant science · 2016
    Article

3 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 1 country.

Jee-Yin AhnDepartment of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.
Xia Liu
Zhixue Liu
Lorena Pereira
Dongmei Cheng
Junmin Peng
Paul A Wade
Anne W Hamburger
Keqiang Ye
Emory University · USUniversity of Maryland, Baltimore · US

Funding

Nuclear GTPase PIKE Regulation and FunctionsR01NS045627 · NINDS · EMORY UNIVERSITY · PI YE, KEQIANG · 2004 to 2013
$3.1M
ERBB RECEPTOR CONTROL OF BREAST CANCER GROWTHR01CA076047 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI HAMBURGER, ANNE W. · 1998 to 2006
$1.7M
NCI NIH HHS R01 CA076047NCI NIH HHS R01 CA76047NINDS NIH HHS R01 NS045627
6 · The paper itself

Abstract

Akt promotes cell survival through phosphorylation. The physiological functions of cytoplasmic Akt have been well defined, but little is known about the nuclear counterpart. Employing a cell-free apoptotic assay and NGF-treated PC12 nuclear extracts, we purified Ebp1 as a factor, which contributes to inhibition of DNA fragmentation by CAD. Depletion of Ebp1 from nuclear extracts or knockdown of Ebp1 in PC12 cells abolishes the protective effects of nerve growth factor, whereas overexpression of Ebp1 prevents apoptosis. Ebp1 (S360A), which cannot be phosphorylated by PKC, barely binds Akt or inhibits DNA fragmentation, whereas Ebp1 S360D, which mimics phosphorylation, strongly binds Akt and suppresses apoptosis. Further, phosphorylated nuclear but not cytoplasmic Akt interacts with Ebp1 and enhances its antiapoptotic action independent of Akt kinase activity. Moreover, knocking down of Akt diminishes the antiapoptotic effect of Ebp1 in the nucleus. Thus, nuclear Akt might contribute to suppressing apoptosis through interaction with Ebp1.

Indexed as

DNA FragmentationAdaptor Proteins, Signal TransducingAnimalsApoptosisCell NucleusDeoxyribonucleasesEnzyme ActivationMultiprotein ComplexesNerve Growth FactorNuclear ProteinsPC12 CellsPoly-ADP-Ribose Binding ProteinsProtein Kinase CProto-Oncogene Proteins c-aktRatsSubcellular FractionsAdaptor Proteins, Signal TransducingDeoxyribonucleasesDffb protein, ratMultiprotein ComplexesNerve Growth FactorNuclear ProteinsPA2G4 protein, ratPoly-ADP-Ribose Binding ProteinsProtein Kinase CProto-Oncogene Proteins c-akt

Identifiers

PMID16642037
PMCPMC1462972
OpenAlexW2151234510

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.