Amy Barrios
University of Utah, UT·Biochemistry
Cells pass messages by attaching phosphate groups to proteins and later removing them. Kinases, the enzymes that add phosphates, are fairly well understood.
- Fields
Biochemistry
Chemistry
Pharmacology
- Topics
protein phosphatases
receptor tyrosine phosphatases
LAR phosphatases
- Grants
- 2 known grants, through Jan 2029
What they work on
- Develop fluorogenic peptide substrates, molecules that fluoresce when cut by an enzyme, that are selective for LAR receptor tyrosine phosphatases, using sequences of their known biological targets, and validate them for use in cells.
- Optimize potent, selective inhibitors of the LAR phosphatase subfamily and use them to probe these enzymes' roles in cellular signaling pathways.
- Identify signaling molecules that bind the outside portion of LAR receptor phosphatases and test how this binding changes phosphatase activity inside the cell.
- Create fluorogenic assays for mammalian histidine kinase and histidine phosphatase activity in cells, and develop the first inhibitors of these enzymes.
- Determine which sequence and structural contexts promote and stabilize phosphohistidine, and how histidine phosphorylation alters protein activity and metal-ion binding.
More about the research
The enzymes that remove phosphates (phosphatases), and the less common phosphorylation of the amino acid histidine, remain much harder to study because good chemical tools are missing. This research builds those tools: fluorogenic substrates, molecules that light up when an enzyme acts on them, and selective inhibitors, molecules that block one enzyme. The goal is to watch and control signaling enzymes in test tubes and in living cells.
Why it matters
Histidine kinases and phosphatases help control G-protein signaling, ion conduction, metabolism and chromatin, and they have been implicated in cardiovascular disease and cancer. Cell-compatible probes and selective inhibitors could help researchers find promising drug targets and lead compounds in these pathways. The probes could also clarify how LAR phosphatases shape signaling during nervous system development.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Niels Bradshaw
Brandeis University, MA·Biochemistry
Uncover general principles of how PPM serine/threonine phosphatases are regulated and directed to the right substrate, using bacterial phosphatases that control the general stress response, a survival pathway linked to virulence.
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.
Caren Freel Meyers
Johns Hopkins University, MD·Biochemistry
Determine how ligand-gated substrate conversion occurs on DXPS, the thiamin diphosphate-dependent enzyme that makes the metabolite DXP, comparing enzymes from different bacterial species.
The school
University of Utah: 58 labs on PI Pages, $789M a year on research, 366 research doctorates a year.
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