Evidence map›Paper›PMID 20819079›Full record

ArticleThe Biochemical journal2010

Unique functions for protein kinase D1 and protein kinase D2 in mammalian cells.

Sharon A Matthews, Maria N Navarro, Linda V Sinclair, Elizabeth Emslie, Carmen Feijoo-Carnero, Doreen A Cantrell

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

60 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Potential role for protein kinase D inhibitors in prostate cancer.Journal of molecular medicine (Berlin, Germany) · 2023
    Review
  7. PKD autoinhibition inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Loss of Protein Kinase D2 Activity Protects Against Bleomycin-Induced Dermal Fibrosis in Mice.Laboratory investigation; a journal of technical methods and pathology · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Dark-Side of Exosomes.Advances in experimental medicine and biology · 2021
    Article
  18. Article
  19. Article
  20. Obesity ofDiabetes, metabolic syndrome and obesity : targets and therapy · 2020
    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

6 authors at 2 institutions in 1 country.

Sharon A MatthewsNinewells Hospital, University of Dundee, Scotland, UK.
Maria N Navarro
Linda V Sinclair
Elizabeth Emslie
Carmen Feijoo-Carnero
Doreen A Cantrell
University of Dundee · GBNinewells Hospital · GB

Funding

Cancer Research UK 10272Wellcome Trust 065975
6 · The paper itself

Abstract

Mammalian PKD (protein kinase D) isoforms have been implicated in the regulation of diverse biological processes in response to diacylglycerol and PKC (protein kinase C) signalling. To compare the functions of PKD1 and PKD2 in vivo, we generated mice deficient in either PKD1 or PKD2 enzymatic activity, via homozygous expression of PKD1(S744A/S748A) or PKD2(S707A/S711A) 'knockin' alleles. We also examined PKD2-deficient mice generated using 'gene-trap' technology. We demonstrate that, unlike PKD1, PKD2 catalytic activity is dispensable for normal embryogenesis. We also show that PKD2 is the major PKD isoform expressed in lymphoid tissues, but that PKD2 catalytic activity is not essential for the development of mature peripheral T- and B-lymphocytes. PKD2 catalytic activity is, however, required for efficient antigen receptor-induced cytokine production in T-lymphocytes and for optimal T-cell-dependent antibody responses in vivo. Our results reveal a key in vivo role for PKD2 in regulating the function of mature peripheral lymphocytes during adaptive immune responses. They also confirm the functional importance of PKC-mediated serine phosphorylation of the PKD catalytic domain for PKD activation and downstream signalling and reveal that different PKD family members have unique and non-redundant roles in vivo.

Indexed as

AnimalsBlotting, WesternCD4-Positive T-LymphocytesCD8-Positive T-LymphocytesCell ProliferationCells, CulturedCytokinesEmbryonic DevelopmentFemaleFlow CytometryGene Expression ProfilingGene Expression Regulation, DevelopmentalLymphocytesLymphoid TissueMaleMiceCytokinesProtein Kinase Cprotein kinase DProtein Kinase D2Protein KinasesReceptors, Antigen, T-Cell

Identifiers

PMID20819079
PMCPMC2995424
OpenAlexW2016870453

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.