Mehdi Mollapour
Upstate Medical University, NY·Biochemistry
Proteins must fold into the right shape before they can work. Heat Shock Protein 90 (Hsp90) is a "chaperone" that helps many signaling proteins, called its clients, fold and stay active.
- Fields
Biochemistry
Pharmacology
Biophysics
- Topics
Hsp90
heat shock protein
molecular chaperone
- Grants
- 1 known grant, through Dec 2026
What they work on
- Determine how the co-chaperones FNIP1, FNIP2 and Tsc1 slow the Hsp90 chaperone cycle and help fold kinase and non-kinase client proteins, using biochemical and biophysical assays.
- Test how chemical tags such as phosphorylation, O-GlcNAcylation, SUMOylation and ubiquitination regulate these co-chaperones and Hsp90 itself.
- Define how co-chaperones and Hsp90 acetylation interact and compensate for one another, building on the finding that loss of Tsc1 reduces Hsp90 acetylation and increases its ATP-breaking activity.
- Determine how this regulatory network affects Hsp90's binding to inhibitor drugs and the sensitivity of cells to these drugs, using cell-based assays.
More about the research
Because many of these clients drive cancer, neurodegeneration, and autoimmune and inflammatory diseases, drugs that block Hsp90 are being tested in clinical trials. How best to use these drugs is still unclear, partly because scientists know little about how Hsp90 is controlled inside cells.
Why it matters
Hsp90 inhibitors are being tested in clinical trials for cancer and other diseases, but how best to use them remains unclear. Knowing which co-chaperones and chemical tags make cells more sensitive to these drugs could suggest ways to increase their potency. It could also help identify which patients' cells are most likely to respond.
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.
Daniel Gewirth
University at Buffalo, NY·Biochemistry
Produce Grp94, the ER chaperone of the hsp90 family, with controlled glycosylation at each of its sequons (sugar-attachment sites), using the lab's in-cell expression system.
Stephanie Gates
University of Missouri-Columbia, MO·Biochemistry
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.
The school
Upstate Medical University: 7 labs on PI Pages, $59M a year on research, 23 research doctorates a year.
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