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Related Experiment Videos

Multiple GTP-binding proteins from cholinergic synaptic vesicles.

J K Ngsee1, K Miller, B Wendland

  • 1Department of Biological Sciences, Stanford University, California 94305.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|January 1, 1990
PubMed
Summary
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Marine ray synaptic vesicles contain distinct GTP-binding proteins. These proteins, identified by molecular weight, are modified by bacterial toxins, revealing their functional roles in cholinergic signaling.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Cholinergic synaptic vesicles are crucial for neurotransmission.
  • GTP-binding proteins play vital roles in cellular signaling pathways.

Purpose of the Study:

  • To identify and characterize GTP-binding proteins within cholinergic synaptic vesicles from Discopyge ommata.
  • To investigate the modification of these proteins by bacterial toxins.

Main Methods:

  • Purification of cholinergic synaptic vesicles from the electric organ of Discopyge ommata.
  • Detection of GTP-binding proteins using alpha 32P-GTP overlay technique.
  • Covalent modification assays with bacterial toxins (pertussis toxin and botulinum toxin).

Main Results:

Related Experiment Videos

  • Two size classes of GTP-binding proteins were identified: higher molecular weight (37-41 kDa) and lower molecular weight (20-29 kDa).
  • Higher molecular weight GTP-binding proteins were ADP-ribosylated by pertussis toxin.
  • Two lower molecular weight GTP-binding proteins were sensitive to botulinum toxin.

Conclusions:

  • Cholinergic synaptic vesicles contain diverse GTP-binding proteins with distinct molecular weights.
  • These proteins are targets for specific bacterial toxins, suggesting roles in vesicle function and regulation.