Evidence map›Paper›PMID 8058779›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

A third synaptotagmin gene, Syt3, in the mouse.

B S Hilbush, J I Morgan

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Neuronal expression of synaptotagmin-related gene 1 is regulated by thyroid hormone during cerebellar development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  11. Deficits in memory and motor performance in synaptotagmin IV mutant mice.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  12. Article
  13. Article
  14. A novel seizure-induced synaptotagmin gene identified by differential display.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  15. Thyroid hormone-responsive genes in developing cerebellum include a novel synaptotagmin and a hairless homolog.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996
    Article
  16. Identification of a nonneuronal isoform of synaptotagmin.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  17. Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  18. Two components of transmitter release at a central synapse.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  19. Review
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

2 authors at 1 institution in 1 country.

B S HilbushRoche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.
J I Morgan
La Roche College · US

Funding

NINDS NIH HHS NS 09053
6 · The paper itself

Abstract

The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca2+ sensors in the process of vesicular trafficking and exocytosis. Results from antibody microinjection and gene-disruption experiments have led to a controversy over whether synaptotagmins are essential for neurotransmission. However, the studies casting doubt on the role of synaptotagmins have assumed that no further isoforms of these molecules exist. Here we report the isolation of a third member of the synaptotagmin family (Syt3) from mouse brain. Although retaining the characteristic five-domain structure of the other synaptotagmins, SYT3 is considerably more divergent at the level of amino acid sequence. In the most highly conserved C2 domain, the mammalian synaptotagmins, SYT1 and SYT2, share 88% sequence identity, whereas SYT3 has only approximately 45% identity to either. Overall, SYT3 has the greatest sequence identity with rat SYT2 and marine ray p65A (both 37%), although homology to all of the known synaptotagmins is > 30%. However, SYT3 is most like p65C when comparing domain structure. Syt3 is expressed in many regions of the nervous system but is undetectable in extraneural tissues. The three murine synaptotagmins have differential expression patterns in the brain. Furthermore, in PC12 cells, Syt3 is coexpressed with Syt1 and is more abundant than the latter. This result suggests that individual neurons may have specific combinations of synaptotagmins that could provide for diversity in vesicular release.

Indexed as

Calcium-Binding ProteinsGene ExpressionAmino Acid SequenceAnimalsBase SequenceBrainDatabases, FactualDNA PrimersMembrane GlycoproteinsMiceMolecular Sequence DataNerve Tissue ProteinsOrgan SpecificityPolymerase Chain ReactionRatsRestriction MappingCalcium-Binding ProteinsDNA PrimersMembrane GlycoproteinsNerve Tissue ProteinsRNA, MessengerSynaptotagmin ISynaptotagminsSyt1 protein, mouseSyt3 protein, mouseSyt3 protein, rat

Identifiers

PMID8058779
PMCPMC44572
OpenAlexW2000839516

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.