Evidence map›Paper›PMID 15367680›Full record

ArticleMolecular and cellular biology2004

Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions.

Gidi Shani, Lea Marash, Devrim Gozuacik, Shani Bialik, Lior Teitelbaum, Galit Shohat, Adi Kimchi

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

43 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Review
  3. Role of ZIP kinase in development of myofibroblast differentiation from HPMCs.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Autophagy and liver cancer.The Turkish journal of gastroenterology : the official journal of Turkish Society of Gastroenterology · 2018
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Autophagy-Regulating microRNAs and Cancer.Frontiers in oncology · 2017
    Review
  16. Article
  17. Article
  18. Involvement of Membrane Blebbing in Immunological Disorders and Cancer.Medical principles and practice : international journal of the Kuwait University, Health Science Centre · 2016
    Review
  19. Article
  20. Review
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

7 authors at 1 institution in 1 country.

Gidi ShaniDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Lea Marash
Devrim Gozuacik
Shani Bialik
Lior Teitelbaum
Galit Shohat
Adi Kimchi
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The death-associated protein (DAP) kinase family includes three protein kinases, DAP kinase, DAP kinase-related protein 1, and ZIP kinase, which display 80% amino acid identity within their catalytic domains and are functionally linked to common subcellular changes occurring during cell death, such as the process of membrane blebbing. Here we show physical and functional cross talk between DAP kinase and ZIP kinase. The two kinases display strong synergistic effects on cell death when coexpressed and physically bind each other via their catalytic domains. Furthermore, DAP kinase phosphorylates ZIP kinase at six specific sites within its extracatalytic C-terminal domain. ZIP kinase localizes to both the nucleus and the cytoplasm and fractionates as monomeric and trimeric forms. Significantly, modification of the DAP kinase phosphorylation sites influences both the localization and oligomerization status of ZIP kinase. A mutant ZIP kinase construct, in which the six serine/threonine residues were mutated to aspartic acid to mimic the phosphorylated state, was found predominantly in the cytoplasm as a trimer and possessed greater cell death-inducing potency. This suggests that DAP kinase and ZIP kinase function in a biochemical pathway in which DAP kinase activates the cellular function of ZIP kinase through phosphorylation, leading to amplification of death-promoting signals.

Indexed as

ApoptosisApoptosis Regulatory ProteinsCalcium-Calmodulin-Dependent Protein KinasesDeath-Associated Protein KinasesGenes, ReporterHeLa CellsHumansMutationPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryTransfectionApoptosis Regulatory ProteinsCalcium-Calmodulin-Dependent Protein KinasesDeath-Associated Protein KinasesProtein Serine-Threonine Kinases

Identifiers

PMID15367680
PMCPMC516725
OpenAlexW2146969546

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.