Evidence map›Paper›PMID 19240038›Full record

ArticleThe Journal of biological chemistry2009

Calpain hydrolysis of alpha- and beta2-adaptins decreases clathrin-dependent endocytosis and may promote neurodegeneration.

Nikita Rudinskiy, Yulia Grishchuk, Anne Vaslin, Julien Puyal, André Delacourte, Harald Hirling, Peter G H Clarke, Ruth Luthi-Carter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Cells · 2026
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  3. Review
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  5. Article
  6. Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Putting a brake on synaptic vesicle endocytosis.Cellular and molecular life sciences : CMLS · 2017
    Review
  16. Article
  17. Review
  18. Article
  19. The Role of PICALM in Alzheimer's Disease.Molecular neurobiology · 2015
    Review
  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

8 authors at 3 institutions in 2 countries.

Nikita RudinskiyBrain Mind Institute, Ecole Polytechnique Fédérale de Lausanne, Station 15, Lausanne CH1015, Switzerland.
Yulia Grishchuk
Anne Vaslin
Julien Puyal
André Delacourte
Harald Hirling
Peter G H Clarke
Ruth Luthi-Carter
École Polytechnique Fédérale de Lausanne · CHUniversity of Lausanne · CHCentre de Recherche Jean Pierre Aubert · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clathrin-dependent endocytosis is mediated by a tightly regulated network of molecular interactions that provides essential protein-protein and protein-lipid binding activities. Here we report the hydrolysis of the alpha- and beta2-subunits of the tetrameric adaptor protein complex 2 by calpain. Calcium-dependent alpha- and beta2-adaptin hydrolysis was observed in several rat tissues, including brain and primary neuronal cultures. Neuronal alpha- and beta2-adaptin cleavage was inducible by glutamate stimulation and was accompanied by the decreased endocytosis of transferrin. Heterologous expression of truncated forms of the beta2-adaptin subunit significantly decreased the membrane recruitment of clathrin and inhibited clathrin-mediated receptor endocytosis. Moreover, the presence of truncated beta2-adaptin sensitized neurons to glutamate receptor-mediated excitotoxicity. Proteolysis of alpha- and beta2-adaptins, as well as the accessory clathrin adaptors epsin 1, adaptor protein 180, and the clathrin assembly lymphoid myeloid leukemia protein, was detected in brain tissues after experimentally induced ischemia and in cases of human Alzheimer disease. The present study further clarifies the central role of calpain in regulating clathrin-dependent endocytosis and provides evidence for a novel mechanism through which calpain activation may promote neurodegeneration: the sensitization of cells to glutamate-mediated excitotoxicity via the decreased internalization of surface receptors.

Indexed as

EndocytosisAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex beta SubunitsAdaptor Proteins, Vesicular TransportAlzheimer DiseaseAnimalsBrainBrain IschemiaCalciumCalpainCell LineCell MembraneClathrinFemaleGlutamic AcidHumansAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex beta SubunitsAdaptor Proteins, Vesicular TransportCalciumCalpainClathrinepsinGlutamic AcidMembrane LipidsMonomeric Clathrin Assembly ProteinsPICALM protein, humanPicalm protein, rat

Identifiers

PMID19240038
PMCPMC2673311
OpenAlexW2028776131

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.