Evidence map›Paper›PMID 1332055›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

DdPK3, which plays essential roles during Dictyostelium development, encodes the catalytic subunit of cAMP-dependent protein kinase.

S K Mann, W M Yonemoto, S S Taylor, R A Firtel

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
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  10. Novel isoform of the Xenopus tropicalis PKA catalytic alpha subunit: An example of alternative splicing.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2010
    Article
  11. Article
  12. Article
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  14. Article
  15. Article
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  17. Role of PKA in the timing of developmental events in Dictyostelium cells.Microbiology and molecular biology reviews : MMBR · 1998
    Review
  18. Article
  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

4 authors.

S K MannDepartment of Biology, University of California, San Diego, La Jolla 92093-0634.
W M Yonemoto
S S Taylor
R A Firtel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously reported the analysis of DdPK3, a developmentally regulated putative serine/threonine kinase that shares approximately 50% amino acid sequence identity with metazoan cAMP-dependent protein kinase A (PKA) and protein kinase C, within their catalytic domains. Cells in which the DdPK3 gene has been disrupted do not aggregate but they are able to induce aggregation-stage genes in response to cAMP pulses and the prestalk-specific ras gene DdrasD in response to high continuous levels of cAMP but will not induce prespore gene expression. In this report, we present conclusive evidence that DdPK3 encodes the catalytic subunit of the Dictyostelium PKA. DdPK3 null cells lack kinase activity that phosphorylates a PKA-specific substrate and is specifically inhibitable by recombinant cAMP-dependent protein kinase inhibitor. DdPK3 expressed in Escherichia coli has PKA activity that is inhibitable by protein kinase inhibitor. When Ddpk3 null cells are complemented with DdPK3 expressed from an actin promoter on an extrachromosomal vector (low copy number), PKA activity is restored and the cells proceed to the slug stage but will not culminate, suggesting that properly regulated PKA activity is essential for culmination. Moreover, overexpressing DdPK3 in wild-type cells on integrating vectors (high copy number) from either an actin or prespore-specific promoter results in accelerated development and the ability to form mature spores in monolayer culture in the presence of high cAMP, a developmental potential lacking in wild-type cells.

Indexed as

8-Bromo Cyclic Adenosine MonophosphateAmino Acid SequenceAnimalsBinding SitesCloning, MolecularCyclic AMPDictyosteliumEscherichia coliGene ExpressionGenetic VectorsKineticsMacromolecular SubstancesMiceMolecular Sequence DataProtein KinasesSequence Homology, Amino Acid8-Bromo Cyclic Adenosine MonophosphateCyclic AMPMacromolecular SubstancesProtein Kinases

Identifiers

PMID1332055
PMCPMC50409

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.