Patrick received his Ph.D. from Harvard University in 1999 after working in the laboratory of Dr. Li-Huei Tsai. He was a Damon Runyon Cancer Research Foundation and a United Negro College Fund/Merck postdoctoral fellow with Erin Schuman at the California Institute of Technology. Patrick joined the faculty in 2004.
Areas of Expertise (7)
Protein Synthesis and Degradation
Lewy Body Disease
Harvard University: Ph.D. 1999
- Damon Runyon Cancer Research Foundation : Postdoctoral Fellow
- United Negro College Fund/Merck : Postdoctoral Fellow
Media Appearances (3)
Issues Of Identity: In Conversation With Hilton Als
The public event will be a conversation between Als and Dr. Gentry Patrick, UC San Diego professor of neurobiology about UC San Diego's production of "A Raisin in the Sun."
Produced on Broadway in 1959, the play explores issues of identity that still resonate. The conversation will focus on issues of racial identity, gender and access to the American dream...
First Person: Telling Students They, Too, Can Go From Compton To Neurobiology
According to Gentry Patrick, you could not have predicted he would become a professor.
“In part because my mom had me at 16 years old,” Patrick said. “I grew up in inner-city, South Central (Los Angeles). I was the first to go to college in my family. Nobody knew about science.”
Patrick is now a full professor and neurobiologist in UC San Diego’s Division of Biological Sciences. His lab studies how the brain turns over proteins that are no longer needed, and how that process is linked to diseases like Alzheimer’s and Parkinson’s...
Lysosome Traffic To Dendritic Spines Is Activity-dependent
“Previously there was no reason to think that lysosomes could travel out to the ends of dendrites at synapses. We are showing neuronal activity is delivering them to the synapse and they are playing an integral and instructive role in remodeling and plasticity, which are so important for learning and memory.”...
Research Focus (1)
Our laboratory is interested in how synaptic activity modulates the molecular make-up of synaptic connections in the mammalian central nervous system (CNS), which in many cases leads to long-lasting changes in synaptic efficacy. The concerted regulation of protein synthesis and degradation is fundamental for the control of diverse cellular events. Many studies have provided evidence that new protein synthesis likely takes place at synapses and is required for plasticity. Protein degradation, on the other hand, provides another way to regulate protein levels. In fact the ability to dynamically control protein levels allows for very tight control of rapid signaling cascades.
We study the ubiquitin-proteasome system (UPS), one of the major cellular pathways controlling protein turnover in mammalian cells. The UPS is a complex proteolytic pathway whereby proteins are targeted to the 26S proteasome for degradation. Ubiquitin is covalently attached to a target protein through a series of steps: first an E1 ubiquitin activating enzymes pass ubiquitin to E2 transferase and E3 ligases. At this point, many times in concert with the help of an E2 enzyme, the E3 ligase binds and modifies the target protein with the ubiquitin. Multiple ubiquitin molecules are added and the protein is recognized and degraded by the 26S proteasome. Many cellular roles have been defined for the UPS such as cell cycle control, cell fate and growth determination, antigen presentation, and many cell signaling pathways. In contrast the mechanisms of how the UPS regulates the growth and development, maintenance, and remodeling of synaptic connection in the mammalian central nervous system (CNS) is less understood.
An interesting problem is how activated synapses of a single neuron become selectively modified as a result of synaptic plasticity. It is known, for example, that synaptic modifications can occur selectively at one group of synapses, but not at another group of synapses on the same neuron. This property is known as "input-" or "synapse specificity". It is plausible that the selective degradation of proteins that restrict or limit plasticity may be required for these synaptic changes to occur. Alternatively, various proteolytic activities may provide specificity for long-term synaptic changes. This could be accomplished through the degradation of some proteins at specific locations or by targeting regulatory components of a proteolytic pathway to modified or unmodified sites.
Goo, M.S., Sancho, L., Slepak, N.; Boassa, D.; Deerinck, T.J., Ellisman, M.H., Bloodgood, B.L., and Patrick, G.N.
2017 In Press
Marquez-Lona, E.M., Torres-Machorro, A.L., Gonzalez, F., S., Pillus, L., Patrick, G.N.
2017 In Press
Dwyer, C.A, Scudder, S.L., Lin, Y., Dozier, L.A., Phan; D., Allen, N. J., Patrick, G.N. and Jeffrey D., J.D.
Cifelli JL, Dozier L, Chung T, Patrick GN, Yang J.
Rodrigues EM, Scudder SL, Goo MS, Patrick GN.