Evidence map›Paper›PMID 17324930›Full record

ArticleThe Journal of biological chemistry2007

Regulation of death-associated protein kinase. Stabilization by HSP90 heterocomplexes.

Liguo Zhang, Kenneth P Nephew, Patricia J Gallagher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  14. Review
  15. Death associated protein kinases: molecular structure and brain injury.International journal of molecular sciences · 2013
    Review
  16. The therapeutic target Hsp90 and cancer hallmarks.Current pharmaceutical design · 2013
    Review
  17. Review
  18. Article
  19. Article
  20. Mind bomb 1 regulation of cFLIP interactions.American journal of physiology. Cell physiology · 2009
    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

3 authors at 2 institutions in 1 country.

Liguo ZhangDepartment of Cellular and Integrated Physiology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.
Kenneth P Nephew
Patricia J Gallagher
Indiana University School of MedicineIndiana University – Purdue University Indianapolis · US

Funding

DNA Methylation and Ovarian CancerR01CA085289 · NCI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI NEPHEW, KENNETH P · 2002 to 2012
$2.4M
Regulation of Apoptosis by DAPKR01HL054118 · NHLBI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI GALLAGHER, PATRICIA J · 1997 to 2006
$1.6M
Regulation of receptor trafficking by myosin IIR01DK062810 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI GALLAGHER, PATRICIA J · 2005 to 2009
$1.5M
NCI NIH HHS CA085289NCI NIH HHS R01 CA085289NHLBI NIH HHS HL54118NHLBI NIH HHS R01 HL054118NIDDK NIH HHS DK062810NIDDK NIH HHS R01 DK062810
6 · The paper itself

Abstract

Death-associated protein kinase (DAPK) has been found associated with HSP90, and inhibition of HSP90 with 17-alkylamino-17-demethoxygeldanamycin reduced expression of DAPK. These results were extended to determine whether the degradation of DAPK in the absence of HSP90 activity is dependent on the ubiquitin-proteasome pathway. Our results show that treatment of cells with geldanamycin (GA) leads to degradation of DAPK, and this degradation is attenuated by the proteasome inhibitor, lactacystin. GA-induced DAPK degradation is also dependent on phosphorylation of DAPK at Ser(308), and the cellular levels of phospho(Ser(308))-DAPK dramatically increase in response to GA treatment. Expression of two distinct ubiquitin E3 ligases, carboxyl terminus of HSC70-interacting protein (CHIP) or DIP1/Mib1, enhanced DAPK degradation, and conversely, short interfering RNA depletion of either CHIP or DIP1/Mib1 attenuated DAPK degradation. In vitro ubiquitination assays confirmed that DAPK is targeted for ubiquitination by both CHIP and DIP. Consistent with these results, DAPK is found in two distinct immune complexes, one containing HSP90 and CHIP and a second complex containing only DIP1/Mib. Collectively, these results indicate that strict modulation of DAPK activities is critical for regulation of apoptosis and cellular homeostasis.

Indexed as

Gene Expression Regulation, EnzymologicApoptosisApoptosis Regulatory ProteinsBenzoquinonesCalcium-Calmodulin-Dependent Protein KinasesCatalysisDeath-Associated Protein KinasesHeLa CellsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicProteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiaryRecombinant ProteinsApoptosis Regulatory ProteinsBenzoquinonesCalcium-Calmodulin-Dependent Protein KinasesDeath-Associated Protein KinasesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLactams, MacrocyclicProteasome Endopeptidase ComplexRecombinant ProteinsSerinetanespimycinUbiquitin

Identifiers

PMID17324930
PMCPMC2823631
OpenAlexW2028200399

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.