Evidence map›Paper›PMID 8195285›Full record

ArticleThe Journal of cell biology1994

Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells.

T Galli, T Chilcote, O Mundigl, T Binz, H Niemann, P De Camilli

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

92 citing papers in PubMed, 226 citations in OpenAlex.

  1. Vamp3/syntaxin 4 mediates the basolateral membrane fusion of TfR transcytosis across the BBB and is exploited by pathogenicProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. FromCells · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Novel function for AP-1B during cell migration.Molecular biology of the cell · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Rab13 Traffics on Vesicles Independent of Prenylation.The Journal of biological chemistry · 2016
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

32 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

T GalliDepartment of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510.
T Chilcote
O Mundigl
T Binz
H Niemann
P De Camilli
Yale University · US

Funding

ROLE OF YPT5 INTERACTING COMPONENTS IN ENDOCYTOSISP01CA046128 · NCI · YALE UNIVERSITY · PI NOVICK, PETER JAY · 1988 to 2007
$9.5M
MECHANISMS OF SECRETION FROM NEURONS AND ENDOCRINE CELLSR01MH045191 · NIMH · YALE UNIVERSITY · PI DE CAMILLI, PIETRO V · 1990 to 1992
–
NCI NIH HHS P01-CA46128NIMH NIH HHS MH45191
6 · The paper itself

Abstract

Cellubrevin is a member of the synaptobrevin/VAMP family of SNAREs, which has a broad tissue distribution. In fibroblastic cells it is concentrated in the vesicles which recycle transferrin receptors but its role in membrane trafficking and fusion remains to be demonstrated. Cellubrevin, like the synaptic vesicle proteins synaptobrevins I and II, can be cleaved by tetanus toxin, a metallo-endoprotease which blocks neurotransmitter release. However, nonneuronal cells are unaffected by the toxin due to lack of cell surface receptors for its heavy chain. To determine whether cellubrevin cleavage impairs exocytosis of recycling vesicles, we tested the effect of tetanus toxin light chain on the release of preinternalized transferrin from streptolysin-O-perforated CHO cells. The release was found to be temperature and ATP dependent as well as NEM sensitive. Addition of tetanus toxin light chain, but not of a proteolytically inactive form of the toxin, resulted in a partial inhibition of transferrin release which correlated with the toxin-mediated cleavage of cellubrevin. The residual release of transferrin occurring after complete cellubrevin degradation was still ATP dependent. Our results indicate that cellubrevin plays an important role in the constitutive exocytosis of vesicles which recycle plasmalemma receptors. The incomplete inhibition of transferrin release produced by the toxin suggests the existence of a cellubrevin-independent exocytotic mechanism, which may involve tetanus toxin-insensitive proteins of the synaptobrevin/VAMP family.

Indexed as

AnimalsCHO CellsCricetinaeExocytosisFluorescent Antibody TechniqueMembrane FusionMembrane ProteinsReceptors, TransferrinTetanus ToxinTransferrinVesicle-Associated Membrane Protein 3Membrane ProteinsReceptors, TransferrinTetanus ToxinTransferrinVesicle-Associated Membrane Protein 3

Identifiers

PMID8195285
PMCPMC2120045
OpenAlexW1983791415

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.