Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A third synaptotagmin gene, Syt3, in the mouse

B S Hilbush1, J I Morgan

  • 1Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.

Proceedings of the National Academy of Sciences of the United States of America
|August 16, 1994
PubMed
Summary

Researchers discovered a new synaptotagmin protein, Syt3, in mouse brains. This protein, distinct from known synaptotagmins, suggests diverse combinations of these Ca2+ sensors may regulate neurotransmission.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Long-lasting transcriptional refractoriness triggered by a single exposure to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrimidine.

Neuroscience·2012
Same author

Extracerebellar role for Cerebellin1: modulation of dendritic spine density and synapses in striatal medium spiny neurons.

The Journal of comparative neurology·2010
Same author

Distinct mechanisms of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrimidine resistance revealed by transcriptome mapping in mouse striatum.

Neuroscience·2008
Same author

Temporal mRNA profiles of inflammatory mediators in the murine 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrimidine model of Parkinson's disease.

Neuroscience·2007
Same author

Protein levels of genes encoded on chromosome 21 in fetal Down syndrome brain: challenging the gene dosage effect hypothesis (Part III).

Amino acids·2003
Same author

Purification of Purkinje cells by fluorescence-activated cell sorting from transgenic mice that express green fluorescent protein.

The European journal of neuroscience·2001

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Protein Chemistry

Background:

  • Synaptotagmins are integral membrane proteins of synaptic vesicles.
  • They are believed to function as Ca2+ sensors in vesicular trafficking and exocytosis.
  • Previous studies have debated the essential role of synaptotagmins in neurotransmission due to assumptions about isoform existence.

Purpose of the Study:

  • To report the isolation and characterization of a novel synaptotagmin family member, Syt3, from mouse brain.
  • To investigate the sequence divergence and expression patterns of Syt3.
  • To explore the implications of Syt3 discovery for understanding synaptotagmin diversity in neurotransmission.

Main Methods:

  • Isolation of a novel synaptotagmin protein (Syt3) from mouse brain.

Related Experiment Videos

  • Amino acid sequence analysis and comparison with known synaptotagmins (Syt1, Syt2, p65A, p65C).
  • Analysis of Syt3 expression patterns in different brain regions and PC12 cells.

    • Main Results:

    • A third synaptotagmin member, Syt3, was isolated from mouse brain, exhibiting a distinct sequence divergence, particularly in the C2 domain.
    • Syt3 shows significant sequence differences compared to Syt1 and Syt2, with approximately 45% identity in the C2 domain.
    • Syt3 is expressed in various neural tissues but not extraneural tissues, and it is coexpressed with Syt1 in PC12 cells, often being more abundant.

    Conclusions:

    • The discovery of Syt3 expands the known synaptotagmin family and highlights significant sequence divergence among isoforms.
    • Differential expression patterns and coexpression of synaptotagmins (Syt1, Syt2, Syt3) in the nervous system suggest specialized roles.
    • Individual neurons may utilize specific combinations of synaptotagmins, contributing to the diversity of vesicular release mechanisms and neurotransmission.