Lan Zhu
Medical College of Wisconsin, WI·Biophysics
Cells sense hormones, neurotransmitters, and many drugs through G protein-coupled receptors (GPCRs), proteins that sit in the cell's outer membrane and relay outside signals inward. They control so many body processes that they are major drug targets.
- Fields
Biophysics
Biochemistry
Pharmacology
- Topics
G protein-coupled receptors
receptor activity-modifying proteins
PDZ domain proteins
- Grants
- 1 known grant, through Jul 2030
What they work on
- 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.
- Test how RAMP binding shapes the functional specificity of these receptors, validating structural findings with mutagenesis and cell-based signaling measurements.
- Uncover how GPCRs bind PDZ domain scaffold proteins and other membrane-associated regulators, and how these contacts control receptor retention at the cell surface and turnover.
- Examine how regulator interactions shape the variety and location of GPCR signaling, using advanced fluorescence imaging combined with structural models.
More about the research
Over 350 GPCR structures have been solved, almost all bound to G proteins, their main signaling partners. Much less is known structurally about the other proteins that escort receptors, hold them at the cell surface, or change their behavior. This project asks how such partners decide where a GPCR goes in the cell and which signals it sends.
Why it matters
Many diseases involve GPCRs that are misrouted inside cells or signal abnormally, and GPCRs are already among the most common drug targets. Understanding how helper proteins such as RAMPs and PDZ proteins steer receptors to the cell surface and shape their signals may open new ways to design therapies that correct faulty receptor trafficking and function.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Xiaojing Yang
University of Illinois Chicago, IL·Biophysics
Determine full-length cryo-EM structures of a bacteriophytochrome and a dual-sensor photoreceptor kinase in different signaling states by resolving structural heterogeneity, meaning the mix of shapes the proteins adopt.
Guangyu Wu
Augusta University, GA·Pharmacology
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.
Joseph Santos-Sacchi
Yale University, CT·Biophysics
Determine the cryo-EM structure of prestin, the outer hair cell motor protein behind cochlear amplification, in the expanded state that voltage brings about, complementing the known contracted-state structure.
The school
Medical College of Wisconsin: 17 labs on PI Pages, $360M a year on research, 44 research doctorates a year.
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