Evidence map›Paper›PMID 36982466›Full record

ArticleInternational journal of molecular sciences2023

Legumain Functions as a Transient TrkB Sheddase.

Christoph Holzner, Katharina Böttinger, Constantin Blöchl, Christian G Huber, Sven O Dahms, Elfriede Dall, Hans Brandstetter

Open access · goldFull text read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 48% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Lysosomal Proteases and Their Inhibitors.International journal of molecular sciences · 2024
    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

7 authors at 1 institution in 1 country.

Christoph HolznerDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.ORCID 0000-0001-5834-3485
Katharina BöttingerDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.ORCID 0000-0001-7246-4611
Constantin BlöchlDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.
Christian G HuberDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.ORCID 0000-0001-8358-1880
Sven O DahmsDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.
Elfriede DallDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.
Hans BrandstetterDepartment of Biosciences and Medical Biology, University of Salzburg, Hellbrunner Str. 34, A-5020 Salzburg, Austria.
University of Salzburg · AT

Funding

Austrian Science Fund FWF P 31867
6 · The paper itself

Abstract

While primarily found in endo-lysosomal compartments, the cysteine protease legumain can also translocate to the cell surface if stabilized by the interaction with the RGD-dependent integrin receptor αVβ3. Previously, it has been shown that legumain expression is inversely related to BDNF-TrkB activity. Here we show that legumain can conversely act on TrkB-BDNF by processing the C-terminal linker region of the TrkB ectodomain in vitro. Importantly, when in complex with BDNF, TrkB was not cleaved by legumain. Legumain-processed TrkB was still able to bind BDNF, suggesting a potential scavenger function of soluble TrkB towards BDNF. The work thus presents another mechanistic link explaining the reciprocal TrkB signaling and δ-secretase activity of legumain, with relevance for neurodegeneration.

Indexed as

Brain-Derived Neurotrophic FactorCysteine ProteasesAsparaginyl EndopeptidaseCysteine EndopeptidasesReceptor, trkBSignal TransductionAsparaginyl EndopeptidaseBrain-Derived Neurotrophic FactorCysteine EndopeptidasesCysteine ProteasesReceptor, trkBdimerizationfunctional processinglysomale proteasesneurotrophinstyrosine receptor kinase

Identifiers

PMID36982466
PMCPMC10049731
OpenAlexW4324097558

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read96
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.