Evidence map›Paper›PMID 26553928›Full record

ArticleThe Journal of cell biology2015

Cdc42-dependent actin dynamics controls maturation and secretory activity of dendritic cells.

Anna M Schulz, Susanne Stutte, Sebastian Hogl, Nancy Luckashenak, Diana Dudziak, Céline Leroy, Ignasi Forné, Axel Imhof, Stephan A Müller, Cord H Brakebusch and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

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  10. Dynamin Binding Protein Is Required forFrontiers in physiology · 2019
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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

12 authors at 5 institutions in 2 countries.

Anna M SchulzInstitute for Immunology, Ludwig Maximilians University Munich, 80336 Munich, Germany.
Susanne StutteInstitute for Immunology, Ludwig Maximilians University Munich, 80336 Munich, Germany.
Sebastian HoglDeutsches Zentrum für Neurodegenerative Erkrankungen, 81377 Munich, Germany.
Nancy LuckashenakInstitute for Immunology, Ludwig Maximilians University Munich, 80336 Munich, Germany.
Diana DudziakDepartment of Dermatology, University Hospital of Erlangen, 91052 Erlangen, Germany.
Céline LeroyInstitute for Immunology, Ludwig Maximilians University Munich, 80336 Munich, Germany.
Ignasi FornéAdolf Butenandt Institute, Ludwig Maximilians University Munich, 80336 Munich, Germany.
Axel ImhofAdolf Butenandt Institute, Ludwig Maximilians University Munich, 80336 Munich, Germany.
Stephan A MüllerDeutsches Zentrum für Neurodegenerative Erkrankungen, 81377 Munich, Germany.
Cord H BrakebuschMolecular Pathology Section, Biotech Research and Innovation Center, University of Copenhagen, 2200 Copenhagen, Denmark.
Stefan F LichtenthalerMunich Cluster for Systems Neurology, Ludwig Maximilians University Munich, 80336 Munich, Germany Deutsches Zentrum für Neurodegenerative Erkrankungen, 81377 Munich, Germany Neuroproteomics, Klinikum rechts der Isar, Institute for Advanced Study, Technische Universität München, 80333 Munich, Germany.
Thomas BrockerInstitute for Immunology, Ludwig Maximilians University Munich, 80336 Munich, Germany brocker@lmu.de.
Ludwig-Maximilians-Universität München · DEGerman Center for Neurodegenerative Diseases · DEInstitute for Advanced Study · DEUniversitätsklinikum Erlangen · DEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell division cycle 42 (Cdc42) is a member of the Rho guanosine triphosphatase family and has pivotal functions in actin organization, cell migration, and proliferation. To further study the molecular mechanisms of dendritic cell (DC) regulation by Cdc42, we used Cdc42-deficient DCs. Cdc42 deficiency renders DCs phenotypically mature as they up-regulate the co-stimulatory molecule CD86 from intracellular storages to the cell surface. Cdc42 knockout DCs also accumulate high amounts of invariant chain-major histocompatibility complex (MHC) class II complexes at the cell surface, which cannot efficiently present peptide antigens (Ag's) for priming of Ag-specific CD4 T cells. Proteome analyses showed a significant reduction in lysosomal MHC class II-processing proteins, such as cathepsins, which are lost from DCs by enhanced secretion. As these effects on DCs can be mimicked by chemical actin disruption, our results propose that Cdc42 control of actin dynamics keeps DCs in an immature state, and cessation of Cdc42 activity during DC maturation facilitates secretion as well as rapid up-regulation of intracellular molecules to the cell surface.

Indexed as

ActinsAnimalsAntigen PresentationB7-2 AntigenCathepsinsCD4-Positive T-LymphocytesCell MembraneDendritic CellsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Genes, MHC Class IILysosomesMiceMice, Inbred C57BLMice, TransgenicUbiquitin-Protein LigasesActinsB7-2 AntigenCathepsinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Fbxw7 protein, mouseUbiquitin-Protein Ligases

Identifiers

PMID26553928
PMCPMC4639873
OpenAlexW2098435148

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.