Guangyu Wu
Augusta University, GA·Pharmacology
A newly made protein is useless if it never reaches the right place in the cell. That is a pressing issue for G protein-coupled receptors, a large family of sensors sitting in the cell's outer membrane that detect hormones, neurotransmitters, light and odors, and that are the targets of a large share of prescription drugs.
- Fields
Pharmacology
Biochemistry
Biology
- Topics
G protein-coupled receptors
anterograde trafficking
membrane trafficking
- Grants
- 1 known grant, through Jul 2030
What they work on
- Define how newly identified cargo receptors and protein complexes recruit nascent G protein-coupled receptors into COPII vesicles, the coated carriers that export proteins from the endoplasmic reticulum.
- Test whether ufmylation, a chemical tag added to proteins, regulates receptor movement from the endoplasmic reticulum through the Golgi apparatus to the cell surface, using biochemical and immunochemical assays.
- Determine how post-Golgi carriers that transport receptors on their final leg are formed, and how the exocyst complex tethers them to the plasma membrane, using live-cell imaging of trafficking receptors.
- Identify structural determinants and regulatory proteins that govern sorting and segregation of different G protein-coupled receptors along the biosynthetic pathway.
More about the research
These receptors only work at the cell surface, so when delivery fails they malfunction, and such delivery failures are linked to human disease. Yet how a freshly made receptor travels forward from the endoplasmic reticulum, the factory where membrane proteins are assembled, through the Golgi apparatus, the sorting station, and out to the surface remains poorly understood.
Why it matters
G protein-coupled receptors are the most heavily pursued class of drug targets, and several human diseases arise when these receptors fail to reach the cell surface. Clarifying the molecular steps and regulators that carry newly made receptors from the endoplasmic reticulum to the membrane may open routes to drugs that correct faulty receptor delivery, and the findings should also apply broadly to how cells route other membrane proteins.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Lan Zhu
Medical College of Wisconsin, WI·Biophysics
Determine the structures of non-Class B GPCRs bound to receptor activity-modifying proteins (RAMPs) using cryo-EM, crystallography, and molecular dynamics, to learn how RAMPs control surface localization and ligand recognition.
Julia Von Blume
Yale University, CT·Biology
Define the molecular requirements for chromogranins and Cab45 to form liquid condensates by liquid-liquid phase separation, using reconstituted systems that mimic the chemical environment inside the trans-Golgi Network.
Joachim Seemann
University of Texas Southwestern Medical Center, TX·Biology
Identify and characterize the RNA–golgin scaffolds that link Golgi stacks into a ribbon, focusing on how the golgin GM130 recruits RNA to Golgi membranes, using biochemical and microscopy approaches.
The school
Augusta University: 11 labs on PI Pages, $166M a year on research, 37 research doctorates a year.
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