Stephanie Gates
University of Missouri-Columbia, MO·Biochemistry
Cells constantly decide whether a misfolded protein should be repaired or destroyed. Helper proteins called chaperones refold damaged proteins.
- Fields
Biochemistry
Biophysics
- Topics
protein quality control
molecular chaperones
Hsp70
- Grants
- 1 known grant, through May 2029
What they work on
- Dissect how the Hsp70/CHIP/BAG-1 chaperone complex affects each step of proteasomal degradation, including ubiquitin tagging, substrate binding and breakdown, using in vitro assays with purified proteins.
- Determine cryo-electron microscopy structures that show a substrate protein being handed from chaperones to the 26S proteasome, the cell's protein-shredding machine.
- Track changes in Hsp70's shape during substrate processing with single-molecule FRET, a light-based method, to learn how co-chaperones and the proteasome reshape its behavior.
More about the research
A large machine called the 26S proteasome chops up proteins that are marked for disposal. This balance is called protein quality control, and when it goes wrong it contributes to cancer and neurodegeneration. The two pathways have mostly been studied separately, so it is still unclear how chaperones sort a protein toward folding or toward destruction.
Why it matters
Faulty protein quality control drives diseases such as Huntington's disease and some cancers. Mapping how the Hsp70/CHIP/BAG-1 complex hands harmful proteins like mutant huntingtin or BCR-ABL to the proteasome could point to new ways to speed up the destruction of disease-causing proteins in patients with cancer or neurodegeneration.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Richard Page
Miami University-Oxford, OH·Biochemistry
Determine how the structure and motions of the CHIP/Hsp70 complex decide whether a misfolded protein is refolded by the Hsp70 chaperone or tagged by the CHIP ubiquitin ligase for destruction.
Michael James Emanuele
University of North Carolina at Chapel Hill, NC·Biochemistry
Define the wave of protein destruction occurring in G2 and at the G2-to-mitosis transition, determining which proteins are degraded and when, and how the phosphate-adding enzyme PLK1 controls this program, using proteomics and cell-based assays.
Tom A Rapoport
Harvard University, MA·Biochemistry
Determine how misfolded glycoproteins, proteins carrying sugar chains, are delivered to the Hrd1 complex and moved from the ER interior across the membrane, building on cryo-electron microscopy structures.
The school
University of Missouri-Columbia: 21 labs on PI Pages, $509M a year on research, 260 research doctorates a year.
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