Andrea Galmozzi
University of Wisconsin-Madison, WI·Biochemistry
Cells use small molecules made during metabolism as signals. These signaling metabolites help control cell division, specialization and responses to the environment.
- Fields
Biochemistry
Chemistry
Pharmacology
- Topics
chemoproteomics
chemical biology
metabolomics
- Grants
- 1 known grant, through May 2028
What they work on
- Develop metabolite-like chemical probes and use chemoproteomics to map the proteins that bind nuclear receptor ligands across the proteome and identify their intracellular chaperones.
- Extend the discovery of PGRMC2 as a heme chaperone moving heme from mitochondria to the nucleus to find transport proteins for other ligands, such as fatty acids that activate PPARs.
- Build spatially and time-resolved maps of protein–metabolite interactions, combining chemoproteomics, metabolomics and cellular assays.
- Determine how chaperone-mediated metabolite trafficking affects nuclear receptor gene regulation, using cellular assays and mouse physiology.
More about the research
Many act on nuclear receptors (NRs), proteins that bind a specific molecule and then switch genes on or off. Because these molecules are chemically reactive, cells must tightly control where they are and how much is present. Yet little is known about how they travel from where they are made or enter the cell to the nucleus. Faulty transport may contribute to cancer and to immune, inflammatory and metabolic diseases.
Why it matters
Faulty transport of signaling metabolites has been linked to cancer and to metabolic, immune and inflammatory disorders. Identifying the proteins that deliver nuclear receptor ligands could provide new drug targets. Such drugs could tune nuclear receptor activity by controlling how much ligand reaches the receptor, rather than by acting on the receptor directly.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Stephen Wiley Ragsdale
University of Michigan, MI·Biochemistry
Determine how the heme oxygenase-2 (HO2) catalytic core coordinates heme sequestration with its own lysosomal breakdown during heme deficiency, and test whether inducible HO1 also sequesters heme.
Y. George Zheng
University of Georgia, GA·Biochemistry
Determine the molecular mechanisms and regulation of protein arginine methyltransferase (PRMT) activity, building on the lab's preliminary results.
Seiya Kitamura
Albert Einstein College of Medicine, NY·Chemistry
Couple the SuFEx click-chemistry high-throughput medicinal chemistry platform with covalent ligands, molecules that bond permanently to proteins, to develop chemical probes for individual underexplored proteins that lack distinct binding sites.
The school
University of Wisconsin-Madison: 91 labs on PI Pages, $1.9B a year on research, 854 research doctorates a year.
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