Evidence map›Paper›PMID 10954749›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor.

M Michaut, C N Tomes, G De Blas, R Yunes, L S Mayorga

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-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

24 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. A heterozygous mutation of GALNTL5 affects male infertility with impairment of sperm motility.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Review
  9. Article
  10. Article
  11. Rab27 and Rab3 sequentially regulate human sperm dense-core granule exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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 3 institutions in 1 country.

M MichautLaboratorio de Biologia Celular y Molecular, Instituto de Histologia y Embriologia (IHEM-CONICET), Facultad de Ciencias Médicas, Universidad Nacional de Cuyo, 5500 Mendoza, Argentina.
C N Tomes
G De Blas
R Yunes
L S Mayorga
Instituto de Histología y Embriología de Mendoza · ARConsejo Nacional de Investigaciones Científicas y Técnicas · ARUniversidad Nacional de Cuyo · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The acrosome reaction of spermatozoa is a complex, calcium-dependent, regulated exocytosis. Fusion at multiple sites between the outer acrosomal membrane and the cell membrane causes the release of the acrosomal contents and the loss of the membranes surrounding the acrosome. However, very little is known about the molecules that mediate and regulate this unique fusion process. Here, we show that N-ethylmaleimide-sensitive factor (NSF), a protein essential for most fusion events, is present in the acrosome of several mammalian spermatozoa. Moreover, we demonstrate that calcium-dependent exocytosis of permeabilized sperm requires active NSF. Previously, we have shown that the addition of the active (GTP-bound) form of the small GTPase Rab3A triggers exocytosis in permeabilized spermatozoa. In the present report we show that Rab3A is necessary for calcium-dependent exocytosis. The activation of Rab3A protects NSF from N-ethylmaleimide inhibition and precludes the exchange of the endogenous protein with recombinant dominant negative mutants of NSF. Furthermore, Rab3A activation of acrosomal exocytosis requires active NSF. Our results suggest that, upon calcium stimulation, Rab3A switches to its active GTP-bound form, triggering the formation of a protein complex in which NSF is protected. This process is suggested to be an essential part of the molecular mechanism of membrane fusion leading to the release of the acrosomal contents.

Indexed as

Acrosome ReactionVesicular Transport ProteinsAcrosomeAdenosine TriphosphatasesBacterial ProteinsCalciumCarrier ProteinsCell Membrane PermeabilityExocytosisGuanosine 5'-O-(3-Thiotriphosphate)HumansKineticsMaleN-Ethylmaleimide-Sensitive Proteinsrab3A GTP-Binding ProteinRecombinant ProteinsAdenosine TriphosphatasesBacterial ProteinsCalciumCarrier ProteinsGuanosine 5'-O-(3-Thiotriphosphate)N-Ethylmaleimide-Sensitive Proteinsrab3A GTP-Binding ProteinRecombinant Proteinsstreptolysin OStreptolysinsVesicular Transport Proteins

Identifiers

PMID10954749
PMCPMC27650
OpenAlexW2115102751

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.