Jiahui Wu
University of Massachusetts, MA·Biochemistry
Inside cells, RNA molecules and RNA-binding proteins (RBPs) team up into ribonucleoprotein complexes (RNPs). RNPs control RNA production and editing, stress responses and genome stability.
- Fields
Biochemistry
Chemistry
Biology
- Topics
ribonucleoprotein
RNA-binding proteins
biomolecular condensates
- Grants
- 1 known grant, through Jun 2030
What they work on
- Develop an RNA tag with ultrahigh affinity to accurately identify the RNA-binding proteins that make up ribonucleoprotein complexes and trigger condensate formation.
- Apply a small-molecule-regulated RNA–protein tethering approach to induce and disrupt specific RBP–RNA interactions in living cells, avoiding overexpression artifacts, to test each RBP's role in condensate assembly and disassembly.
- Use a fluorogenic RNA imaging system to track how long noncoding RNA–mRNA interactions contribute to RNP condensate formation during the cellular stress response.
More about the research
Many RNPs gather into condensates, membraneless droplets that form much like oil separating from water, a process called liquid–liquid phase separation. When these condensates go wrong, cancers and neurological disorders can follow. Yet how condensates form, dissolve and are regulated is poorly understood, largely because the right tools are missing. The lab builds chemical biology tools to see what RNPs contain and how they change in living cells. It has already developed a way to track RNA movement in living cells and a method to identify the proteins that bind specific RNA motifs.
Why it matters
Faulty RNP condensates have been implicated in various cancers and neurological disorders. New tools for identifying condensate proteins and tracking RNA in living cells could reveal how these assemblies form and fail. This understanding could eventually point to disease mechanisms and possible targets. The methods could also be adopted by other labs studying RNA biology.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Manuel Ascano
Vanderbilt University, TN·Biochemistry
Identify RNA–protein complexes sorted into extracellular vesicles using EV-CLASP, which crosslinks 4SU-labeled RNAs to their binding proteins, combined with biotin-dependent proximity labeling.
Priya R. Banerjee
University at Buffalo, NY·Biophysics·Early-career
Test whether pioneer transcription factors, proteins that can bind DNA packed into closed chromatin, act by forming liquid-like droplets on DNA that concentrate RNA polymerases and nucleosome-remodeling complexes to switch genes on.
Lin Guo
Thomas Jefferson University, PA·Biochemistry
Determine how the nuclear import receptor Kapβ2 engages and chaperones newly found partner proteins that lack a nuclear localization signal, using cryo-electron microscopy to solve their structures.
The school
University of Massachusetts: 28 labs on PI Pages, $282M a year on research, 337 research doctorates a year.
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