Jeroen Roelofs
University of Kansas, KS·Biochemistry
Cells constantly destroy their own proteins, and the machine that does most of that work is the proteasome, a large barrel-shaped complex that chews up proteins tagged for disposal with a small marker protein called ubiquitin. When a cell is growing comfortably, it has enough proteasomes to keep up.
- Fields
Biochemistry
Biology
Genetics
- Topics
proteasome
protein degradation
ubiquitin
- Grants
- 1 known grant, through Jun 2028
What they work on
- Determine how proteasome-associated assembly factors, including Pba1-Pba2/PAC1-PAC2, Fub1/PI31, and Blm10/PA200, contribute to sequential versus parallel pathways during the early assembly of new proteasome complexes.
- Identify the molecular interactions that drive proteasomes into liquid-liquid phase-separated condensates, using newly identified conditions and regulatory factors that control proteasome condensate formation in budding yeast.
- Test whether condensate formation stores proteasomes, protects them from proteaphagy (their delivery to the cell's recycling machinery), or concentrates them with substrates in degradation centers.
- Test the hypothesis that when proteasome capacity is limited, proteasomes prioritize degrading certain ubiquitin-tagged substrates over others, using in vivo degradation assays and asking how proteasome-associated proteins set that priority.
- Compare these proteasome stress responses between Saccharomyces cerevisiae and mammalian tissue culture cells to establish which mechanisms controlling proteasome levels and composition are evolutionarily conserved.
More about the research
Under stress such as heat or oxidative damage, demand changes, and the cell adjusts its degradation capacity by making more proteasomes, destroying them, or moving them somewhere else. Understanding that adjustment matters because the same stresses accompany aging and diseases including neurodegeneration and cancer. The goal of this work is mechanistic insight into how these different stress responses operate.
Why it matters
The ability to degrade proteins, and several of the factors that regulate it, are implicated in human diseases including neurodegenerative disorders and cancer, and manipulating proteasomes in cells has already proven therapeutically valuable. A molecular account of how cells raise, remove, or relocate proteasomes could provide a foundation for identifying targets and drugs that tune proteasome levels and local activity.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Fei Wang
University of Texas Southwestern Medical Center, TX·Biology
Determine how autophagy, the cell's self-digestion system, promotes gametogenesis in Saccharomyces cerevisiae across meiosis entry, DNA replication, meiosis exit and spore membrane formation, using yeast genetics, biochemistry and imaging.
Jaime Lopez-Mosqueda
University of Texas at Austin, TX·Biochemistry·Early-career
Test for a unifying molecular mark that flags DNA-protein crosslinks for destruction, regardless of the size or chemical nature of the trapped protein, using biochemical and molecular biology approaches.
Jiahui Wu
University of Massachusetts, MA·Biochemistry
Develop an RNA tag with ultrahigh affinity to accurately identify the RNA-binding proteins that make up ribonucleoprotein complexes and trigger condensate formation.
The school
University of Kansas: 26 labs on PI Pages, $546M a year on research, 351 research doctorates a year.
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