Zuoshang Xu
University of Massachusetts Chan Medical School, MA·Neuroscience
Amyotrophic lateral sclerosis (ALS) destroys the motor neurons that control muscles, leading to weakness, paralysis and death. No therapy can stop or reverse it, and why the neurons die remains unclear.
- Fields
Neuroscience
Biochemistry
Medicine & Clinical Research
- Topics
amyotrophic lateral sclerosis
motor neuron disease
neurodegeneration
- Grants
- 1 known grant, through Apr 2027
What they work on
- Map which spinal cord proteins are citrullinated and how this changes across disease stages, using proteomics in SOD1 G93A and PFN1 C71G ALS mouse models.
- Identify the exact citrullination sites on ALS-associated proteins and test whether the enzyme PAD2 is responsible for the altered citrullination in ALS.
- Determine how citrullination affects aggregation and function of ALS-associated proteins, and whether highly citrullinated proteins drive insoluble clumps.
- Examine how protein citrullination is altered in human ALS to test whether the mouse findings carry over to patients.
More about the research
This project, a collaboration between the Xu and Thompson labs, explores a new suspect: citrullination. In this chemical change, enzymes called protein arginine deiminases (PADs) convert the amino acid arginine into citrulline. The change removes a positive charge, which can alter how a protein works and how it binds membranes, nucleic acids and other proteins.
Why it matters
ALS is fatal and has no therapy that halts its progression. Showing that PAD2 and protein citrullination contribute to motor neuron degeneration could open a new treatment route through existing PAD inhibitors. Citrullination changes could also serve as biomarkers for detecting ALS early.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Daniel Lee
University of Kentucky, KY·Neuroscience
Test how the arginine sensor CASTOR1, a brake on the growth regulator mTORC1, improves lysosome function, repair and clearance of protein clumps when cell models are stressed by tau or lysosome-damaging agents.
Jingjing Liang
University of Arizona, AZ·Neuroscience
Test how Aggregatin, a protein encoded by the Alzheimer's-linked gene FAM222A, controls TDP-43 clumping and toxicity in neurons, using Aggregatin knockout models.
Brian Cherrington
University of Wyoming, WY·Microbiology & Immunology
Identify the citrullinome, the full set of citrullinated proteins, in mouse female reproductive tract fluid across the estrous cycle, pregnancy and postpartum.
The school
University of Massachusetts Chan Medical School: 29 labs on PI Pages, $350M a year on research, 55 research doctorates a year.
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