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| Jennifer Morgan |
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Assistant Professor
Ph.D.
e-mail
Office PAT 522
(512)
Morgan Lab home
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The process by which neurons communicate with each other is called
synaptic transmission, and it underlies all human social, cognitive,
motor and sexual behaviors. Communication between neurons occurs at
specialized contact sites, chemical synapses, where one neuron releases
neurotransmitters onto the other neuron. In this way the two neurons
“talk to” one another. Thus, the structural and functional integrity of
synapses must be maintained in order for the neurons to communicate over
the long term. Yet synapses must be dynamic and flexible in order to
adapt to changes in the environment. In my lab, we are exploring the
molecular mechanisms underlying both synaptic maintenance and synaptic
plasticity.
The actin cytoskeleton may be a key player at synapses. In non-neuronal
cells, the actin cytoskeleton can be stable, providing structural
support for a cell, or it can be dynamic, generating the forces that
drive many cellular functions. However, in neurons, particularly at the
pre-synapse, the roles of actin are still unclear. Thus, the current
goals of our research are: 1) to elucidate the roles of presynaptic
actin in synapse maintenance (vesicle trafficking; cell adhesion) and 2)
to determine whether actin participates in synapse regeneration
following axonal injury. My experiments take advantage of the giant
synapses found within axons of the lamprey spinal cord. Each synapse has
a prominent ring of actin surrounding sites of neurotransmitter release,
making this the ideal preparation in which to study presynaptic actin.
We use electrophysiology, imaging, biochemistry, and molecular biology
techniques toward our goals. Recently, we have also developed behavioral
and anatomical assays with which to explore the role of actin during
spinal cord regeneration. Since synaptic actin has been implicated in a
wide variety of neurological and neuromuscular disorders, our studies
have wide-ranging implications for human health.
Actin is present at lamprey giant synapses. A) Confocal image showing a
single lamprey axon injected with a fluorescent marker for actin. Each
actin ring represents a giant synapse. B) Higher magnification image
showing that the actin ring (green) surrounds vesicle clusters (red) at
sites of neurotransmitter release. Bar in each panel equals 5 µm.
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Selected Publications
Morgan JR, Prasad K, Hao W, Augustine GJ, and Lafer EM (2000) A conserved clathrin assembly motif is essential for synaptic vesicle endocytosis. Journal of Neuroscience 20: 8667-8676.
Morgan JR, Prasad K, Jin S, Augustine GJ, and Lafer EM (2001) Uncoating of clathrin-coated vesicles in presynaptic terminals is mediated by auxilin-Hsc70 interaction. Neuron 32:289-300.
Morgan JR, Prasad K, Jin S, Augustine GJ, and Lafer EM (2003) Eps15 homology domain-NPF interactions regulate clathrin coat assembly during synaptic vesicle recycling Journal of Biological Chemistry 278:33583-33592.
Morgan JR, Di Paolo G, Werner H, Shchedrina VA, Pypaert M, Pieribone VA, and De Camilli P (2004) A role for talin in presynaptic function. Journal of Cell Biology 167:43-50.
*Bourne JN, *Morgan JR, Pieribone VA (2006) Actin polymerization regulates clathrin coat maturation during early stages of synaptic vesicle recycling at lamprey synapses. Journal of Comparative Neurology 497:600-609 (* Authors contributed equally).
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