Evidence map›Paper›PMID 10373524›Full record

ArticleMolecular and cellular biology1999

SDF-2 induction of terminal differentiation in Dictyostelium discoideum is mediated by the membrane-spanning sensor kinase DhkA.

N Wang, F Söderbom, C Anjard, G Shaulsky, W F Loomis

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. From environmental sensing to developmental control: cognitive evolution in dictyostelid social amoebas.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
    Article
  5. Review
  6. Review
  7. Article
  8. Extracellular signaling in Dictyostelium.The International journal of developmental biology · 2019
    Review
  9. Evolution of multicellularity in Dictyostelia.The International journal of developmental biology · 2019
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. 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

5 authors.

N WangCenter for Molecular Genetics, Department of Biology, University of California-San Diego, La Jolla, California 92093, USA.
F Söderbom
C Anjard
G Shaulsky
W F Loomis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SDF-2 is a peptide released by prestalk cells during culmination that stimulates prespore cells to encapsulate. Genetic evidence indicates that the response is dependent on the dhkA gene. This gene encodes a member of the histidine kinase family of genes that functions in two-component signal transduction pathways. The sequence of the N-terminal half of DhkA predicts two hydrophobic domains separated by a 310-amino-acid loop that could bind a ligand. By inserting MYC6 epitopes into DhkA, we were able to show that the loop is extracellular while the catalytic domain is cytoplasmic. Cells expressing the MYC epitope in the extracellular domain of DhkA were found to respond only if induced with 100-fold-higher levels of SDF-2 than required to induce dhkA+ cells; however, they could be induced to sporulate by addition of antibodies specific to the MYC epitope. To examine the enzymatic activity of DhkA, we purified the catalytic domain following expression in bacteria and observed incorporation of labelled phosphate from ATP consistent with histidine autophosphorylation. Site-directed mutagenesis of histidine1395 to glutamine in the catalytic domain blocked autophosphorylation. Furthermore, genetic analyses showed that histidine1395 and the relay aspartate2075 of DhkA are both critical to its function but that another histidine kinase, DhkB, can partially compensate for the lack of DhkA activity. Sporulation is drastically reduced in double mutants lacking both DhkA and DhkB. Suppressor studies indicate that the cyclic AMP (cAMP) phosphodiesterase RegA and the cAMP-dependent protein kinase PKA act downstream of DhkA.

Indexed as

PeptidesProtozoan ProteinsAnimalsCatalytic DomainCell DifferentiationCell MembraneDictyosteliumIntercellular Signaling Peptides and ProteinsMembrane ProteinsMutagenesis, Site-DirectedPhosphorylationProtein KinasesProteinsRecombinant Fusion ProteinsDhkA protein, Dictyostelium discoideumDhkB protein, Dictyostelium discoideumIntercellular Signaling Peptides and ProteinsMembrane ProteinsPeptidesProtein KinasesProteinsProtozoan ProteinsRecombinant Fusion ProteinsSDF-2 protein, Dictyostelium discoideum

Identifiers

PMID10373524
PMCPMC84273

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.