Evidence map›Paper›PMID 26507660›Full record

ArticleThe Journal of biological chemistry2016

Protein Kinase D2 Assembles a Multiprotein Complex at the Trans-Golgi Network to Regulate Matrix Metalloproteinase Secretion.

Tim Eiseler, Christoph Wille, Conny Koehler, Anett Illing, Thomas Seufferlein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Potential role for protein kinase D inhibitors in prostate cancer.Journal of molecular medicine (Berlin, Germany) · 2023
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Small Extracellular Vesicles Propagate the Inflammatory Response After Trauma.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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  20. 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

5 authors at 2 institutions in 1 country.

Tim EiselerFrom the Department of Internal Medicine I, Ulm University, Albert Einstein Allee 23, D-89081 Ulm, Germany and tim.eiseler@uniklinik-ulm.de.
Christoph WilleFrom the Department of Internal Medicine I, Ulm University, Albert Einstein Allee 23, D-89081 Ulm, Germany and.
Conny Koehlerthe Department of Internal Medicine I, Martin-Luther University Halle-Wittenberg, Ernst-Grube, Strasse 40, D-06120 Halle (Saale), Germany.
Anett IllingFrom the Department of Internal Medicine I, Ulm University, Albert Einstein Allee 23, D-89081 Ulm, Germany and.
Thomas SeufferleinFrom the Department of Internal Medicine I, Ulm University, Albert Einstein Allee 23, D-89081 Ulm, Germany and thomas.seufferlein@uniklinik-ulm.de.
Universität Ulm · DEMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vesicle formation and fission are tightly regulated at the trans-Golgi network (TGN) during constitutive secretion. Two major protein families regulate these processes: members of the adenosyl-ribosylation factor family of small G-proteins (ARFs) and the protein kinase D (PKD) family of serine/threonine kinases. The functional relationship between these two key regulators of protein transport from the TGN so far is elusive. We here demonstrate the assembly of a novel functional protein complex at the TGN and its key members: cytosolic PKD2 binds ARF-like GTPase (ARL1) and shuttles ARL1 to the TGN. ARL1, in turn, localizes Arfaptin2 to the TGN. At the TGN, where PKD2 interacts with active ARF1, PKD2, and ARL1 are required for the assembly of a complex comprising of ARF1 and Arfaptin2 leading to secretion of matrix metalloproteinase-2 and -7. In conclusion, our data indicate that PKD2 is a core factor in the formation of this multiprotein complex at the TGN that controls constitutive secretion of matrix metalloproteinase cargo.

Indexed as

Adaptor Proteins, Signal TransducingADP-Ribosylation Factor 1ADP-Ribosylation FactorsAnimalsCell LineGuanosine TriphosphateHumansIsoenzymesMatrix Metalloproteinase 2Matrix Metalloproteinase 7Membrane ProteinsMice, Inbred C57BLModels, BiologicalMultiprotein ComplexesProtein BindingProtein Kinase D2Adaptor Proteins, Signal TransducingADP-Ribosylation Factor 1ADP-ribosylation factor related proteinsADP-Ribosylation FactorsARFIP2 protein, humanGuanosine TriphosphateIsoenzymesMatrix Metalloproteinase 2Matrix Metalloproteinase 7Membrane ProteinsMultiprotein ComplexesProtein Kinase D2Protein KinasesADP ribosylation factor (ARF)metalloproteaseprotein kinase D (PKD)secretionvesicles

Identifiers

PMID26507660
PMCPMC4697185
OpenAlexW2156912175

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.