Lin Guo
Thomas Jefferson University, PA·Biochemistry
Cells organize many of their contents without membranes. Some proteins that bind RNA can gather into liquid-like droplets, much as oil separates from water.
- Fields
Biochemistry
Biophysics
Neuroscience
- Topics
liquid-liquid phase separation
biomolecular condensates
RNA-binding proteins
- Grants
- 1 known grant, through Jun 2031
What they work on
- 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.
- Extend miniTurbo-mass spectrometry, a proximity-tagging method that identifies a protein's neighbors in cells, to two additional nuclear import receptors to learn how each regulates condensates in different cell locations.
- Investigate how RNA structure and dynamics control phase separation of RNA-binding proteins such as FUS, using single-molecule fluorescence biophysical methods alongside conventional biochemistry.
- Build on prior work defining how Kapβ2 and Impβ1 suppress phase separation of FUS and TDP-43 to develop the basis for restoring healthy protein phase in cells.
More about the research
This process is called liquid–liquid phase separation (LLPS), and it builds compartments called biocondensates that support normal cell functions. When it goes wrong, these proteins can clump abnormally, and that has been linked to neurodegenerative diseases and cancer. The central question is what keeps this process under control, and whether those natural controls could be used to reverse harmful clumping.
Why it matters
Abnormal clumping of RNA-binding proteins such as FUS and TDP-43 is tied to neurodegenerative diseases and some cancers. Knowing how nuclear import receptors and RNA keep these proteins in a healthy state could support future strategies that strengthen these natural regulators. One example is RNA-based oligonucleotides, short designed RNA strands. Such strategies may help restore normal protein organization in diseased cells.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
John Straub
Boston University, MA·Biophysics
Identify factors that govern liquid-liquid phase separation and later amyloid aggregation of the disordered proteins tau and alpha-synuclein, combining experiments with computer simulations.
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.
Steven L Mcknight
University of Texas Southwestern Medical Center, TX·Biochemistry
Identify and map thousands of distinct labile cross-beta cores, the short segments that nucleate self-association, within low-complexity domains across the human proteome using high-throughput methods.
The school
Thomas Jefferson University: 12 labs on PI Pages, $271M a year on research, 33 research doctorates a year.
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