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Related Experiment Videos

Transmembrane topography and evolutionary conservation of synaptophysin.

P A Johnston1, R Jahn, T C Südhof

  • 1Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235.

The Journal of Biological Chemistry
|January 15, 1989
PubMed
Summary

Synaptophysin, a key synaptic vesicle protein, spans the membrane four times with both ends inside. Its functional regions are highly conserved across species, suggesting an important role.

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Area of Science:

  • Neurobiology
  • Molecular Biology
  • Membrane Protein Structure

Background:

  • Synaptophysin is the primary integral membrane protein of small synaptic vesicles.
  • Its structure suggests four transmembrane regions and a unique carboxyl-terminal domain.

Purpose of the Study:

  • To determine the transmembrane organization of synaptophysin.
  • To investigate the evolutionary conservation of synaptophysin domains based on membrane localization.

Main Methods:

  • Raising five site-specific antipeptide antibodies against synaptophysin.
  • Mapping epitopes using proteolysis susceptibility to determine orientation (cytoplasmic vs. intravesicular).
  • Determining the primary structure of bovine synaptophysin and comparing it with rat and human sequences.

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Main Results:

  • Confirmed a topographic model where synaptophysin spans the synaptic vesicle membrane four times.
  • Both the amino and carboxyl termini of synaptophysin are located on the cytoplasmic side.
  • Intravesicular loops showed 22% amino acid substitutions, while transmembrane and cytoplasmic regions were highly conserved (3% substitutions) across species.

Conclusions:

  • Synaptophysin possesses a well-defined transmembrane topology with cytoplasmic N- and C-termini.
  • The high conservation of transmembrane and cytoplasmic domains suggests their critical functional importance.
  • Functional sites of synaptophysin are likely located in conserved intramembranous and cytoplasmic sequences.