Evidence map›Paper›PMID 9801366›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

SVOP, an evolutionarily conserved synaptic vesicle protein, suggests novel transport functions of synaptic vesicles.

R Janz, K Hofmann, T C Südhof

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Drug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  6. Article
  7. Article
  8. Hidden proteome of synaptic vesicles in the mammalian brain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Synaptic vesicle protein 2: A multi-faceted regulator of secretion.Seminars in cell & developmental biology · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Puzzling Out Synaptic Vesicle 2 Family Members Functions.Frontiers in molecular neuroscience · 2017
    Review
  15. Review
  16. Review
  17. Overlapping functions of stonin 2 and SV2 in sorting of the calcium sensor synaptotagmin 1 to synaptic vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Review
  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

3 authors at 2 institutions in 2 countries.

R JanzCenter for Basic Neuroscience, Department of Molecular Genetics and Howard Hughes Medical Institute, The University of Texas Southwestern Medical School, Dallas, Texas 75235, USA.
K Hofmann
T C Südhof
Howard Hughes Medical Institute · USSwiss Group For Clinical Cancer Research · CH

Funding

FUNCTION OF NEUREXINSR37MH052804 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI SUDHOF, THOMAS C. · 2000 to 2019
$9.3M
Function of NeurexinsR01MH052804 · NIMH · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI SUDHOF, THOMAS C. · 1994 to 2024
$3.7M
NIMH NIH HHS R01 MH052804NIMH NIH HHS R37 MH052804
6 · The paper itself

Abstract

We describe a novel synaptic vesicle protein called SVOP that is distantly related to the synaptic vesicle proteins SV2A, SV2B, and SV2C (20-22% sequence identity). Both SVOP and SV2 contain 12 transmembrane regions. However, SV2 is highly glycosylated, whereas SVOP is not. Databank searches revealed that closely related homologs of SVOP are present in Caenorhabditis elegans and Drosophila (48% sequence identity), suggesting that SVOP is evolutionarily ancient. In contrast, no invertebrate orthologs of SV2 were detected. The sequences of SVOP and SV2 exhibit homology with transport proteins, in particular with mammalian organic cation and anion transporters. SVOP and SV2 are more distantly related to eukaryotic and bacterial phosphate, sugar, and organic acid transporters. SVOP is expressed at detectable levels only in brain and endocrine cells where it is primarily localized to synaptic vesicles and microvesicles. SVOP is present in all brain regions, with particularly high levels in large pyramidal neurons of the cerebral cortex. Immunocytochemical staining of adjacent rat brain sections for SVOP and SV2 demonstrated that SVOP and SV2 are probably coexpressed in most neurons. Although the functions of SV2 and SVOP remain obscure, the evolutionary conservation of SVOP, its hydrophobic nature, and its homology to transporters strongly support a role in the uptake of a novel, as yet unidentified component of synaptic vesicles. Thus synaptic vesicles contain two classes of abundant proteins with 12 transmembrane regions that are related to transporters, nonglycosylated SVOP and highly glycosylated SV2, suggesting that the transport functions of synaptic vesicles may be more complex than currently envisioned.

Indexed as

Conserved SequenceVesicular Transport ProteinsAdrenal GlandsAnimalsAntibodiesBiological TransportCaenorhabditis elegansCarrier ProteinsChromaffin CellsCloning, MolecularCOS CellsDrosophilaEvolution, MolecularGene Expression Regulation, DevelopmentalImmunohistochemistryMembrane GlycoproteinsAntibodiesCarrier ProteinsMembrane GlycoproteinsMembrane ProteinsNerve Tissue ProteinsNeurotransmitter AgentsRNA, MessengerSv2a protein, ratSv2b protein, mouseSv2b protein, ratSvop protein, ratVesicular Transport Proteins

Identifiers

PMID9801366
PMCPMC6792886
OpenAlexW1801554614

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.