Proteins functioning in synaptic transmission at the sensory to motor synapse of Aplysia.
Over expression of Aplysia synaptotagmin in acutely dissected cholinergic neurons from the buccal ganglia, or in primary co-cultures of glutaminergic sensory neurons and motor neurons, causes a reduction synaptic transmission. Anti-sense oligonucleotide treatment of similar cultures produced an enhancement of synaptic transmission. The interaction between Aplysia VAMP/synaptobrevin and syntaxin is reconstructed using the yeast two hybrid system, and used to identify amino acid residues of VAMP/synaptobrevin that are required for this interaction. Point mutations around residue 50, close to the site of cleavage by botulinum toxins specifically disrupt the interaction with syntaxin. An additional VAMP/synaptobrevin binding protein, VAP33, is identified using the yeast two hybrid system. Intracellular injection of VAP33 specific antisera inhibits synaptic transmission in sensory-motor neuron co-cultures.
Skehel
P A
PA
Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.
Armitage
B A
BA
Bartsch
D
D
Hu
Y
Y
Kaang
B K
BK
Siegelbaum
S A
SA
Kandel
E R
ER
Martin
K C
KC
D000595:Amino Acid Sequence; D000818:Animals; D001048:Aplysia; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000032:analysis* / Q000235:genetics; D002478:Cells, Cultured; D008562:Membrane Glycoproteins / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis* / Q000235:genetics; D008969:Molecular Sequence Data; D009046:Motor Neurons; D009419:Nerve Tissue Proteins / Q000032:analysis*; D050683:R-SNARE Proteins; D017386:Sequence Homology, Amino Acid; D009435:Synaptic Transmission / Q000502:physiology*; D050857:Synaptotagmins
D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins; D050857:Synaptotagmins