John Peters
University of Richmond, VA·Neuroscience
Forming a memory depends on neurons strengthening their connections, a process called long-term potentiation. One key step is adding more AMPA receptors, proteins that respond to the neurotransmitter glutamate, to the neuron's surface membrane.
- Fields
Neuroscience
Biochemistry
Biophysics
- Topics
AMPA receptor
AMPAR trafficking
long-term potentiation
- Grants
- 1 known grant, through Feb 2028
What they work on
- Determine what the poorly characterized N-terminal and linker regions of SNAP-47, a SNARE membrane-fusion protein, contribute to vesicle fusion during AMPA receptor delivery, using an in vitro fusion assay with purified components.
- Solve the 3D structure of the SNARE complex of syntaxin-3, synaptobrevin-2 and SNAP-47 that drives AMPA receptor insertion into the neuronal membrane, using single-particle cryo-electron microscopy.
- Identify new proteins that regulate AMPA receptor trafficking by screening postsynaptic proteins for likely binding partners with AlphaFold multimer structure prediction, then confirming the interactions in vitro.
More about the research
The receptors arrive in small internal membrane bubbles, called vesicles, which must fuse with the outer membrane. Membrane fusion that releases neurotransmitters has been studied for decades. The control of fusion that delivers receptors, by contrast, is still poorly understood.
Why it matters
This basic research could explain how neurons control the delivery of AMPA receptors that strengthen synapses during learning. It would add to understanding of synaptic plasticity and memory formation. It may also point to proteins that regulate this step, which could guide future studies of how memory works.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Jason D Shepherd
University of Utah, UT·Neuroscience
Test whether LTP increases Arc protein in dendrites and its assembly into virus-like capsids, using live imaging of neurons.
Yongli Zhang
Yale University, CT·Biophysics
Reconstitute the full primed SNARE complex, adding complexin and the calcium sensor synaptotagmin-1 to Munc18-1, syntaxin-1, VAMP2 and Munc13-1, and characterize its stability, structure and dynamics on membranes.
Edwin R Chapman
University of Wisconsin-Madison, WI·Neuroscience
Measure opening, closing, widening and ion selectivity of single SNARE-formed fusion pores at microsecond resolution, using nanodiscs fused to an artificial lipid membrane and electrical recording.
The school
University of Richmond: 2 labs on PI Pages, $3M a year on research.
Reach out
A start for your email. Fill in the brackets.