Jennifer Kong
University of Washington, WA·Biochemistry
Cells constantly send each other chemical signals to build an embryo, repair tissue and keep adult organs working. Scientists know a lot about how these signals are made and how they trigger responses inside a cell.
- Fields
Biochemistry
Biology
Biomedical Engineering
- Topics
cell signaling
signaling sensitivity
E3 ubiquitin ligase
- Grants
- 1 known grant, through Mar 2031
What they work on
- Define the principles by which membrane-tethered E3 ubiquitin ligases, enzymes that tag proteins for destruction, recognize and target cell-surface receptors, mapping their target networks with mass spectrometry and biochemistry.
- Determine how these membrane-anchored ligases control signaling sensitivity in living tissue, using cell biology approaches and mouse models to connect receptor turnover with development and tissue maintenance.
- Use protein design to build custom small proteins that tune membrane-tethered E3 ligase activity or redirect the ligases to new receptors, creating a programmable platform for degrading chosen surface proteins.
More about the research
They know much less about how a receiving cell turns its sensitivity up or down. One key dial is how many receptors, the proteins that detect signals, sit on the cell surface. The team's own work supports this idea. How cells control receptor turnover and stability is still poorly understood.
Why it matters
Faulty receptor turnover is linked to congenital disorders, neurodegeneration, autoimmunity and tumor growth. Understanding how membrane-tethered E3 ligases control receptor levels, and designing proteins that redirect them, could lay groundwork for therapies that selectively remove disease-causing surface receptors and restore normal cell signaling.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Jaewon Chang
Emory University, GA·Chemistry
Design and synthesize covalent warheads that react with lysine, tyrosine and serine residues on E3 ubiquitin ligases, the enzymes that tag proteins for destruction, going beyond the cysteine-reactive chemistry used so far.
Qiaobing Xu
Tufts University, MA·Biomedical Engineering
Covalently attach a ligand that binds the target protein onto an E3 ligase-related protein, creating a two-part degrader that avoids the PROTAC hook effect.
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.
The school
University of Washington: 81 labs on PI Pages, $1.7B a year on research, 694 research doctorates a year.
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