Jingjing Liang
University of Arizona, AZ·Neuroscience
In several brain diseases, a protein called TDP-43 leaves the cell nucleus, where it normally works, and forms clumps in the surrounding cytoplasm. This misplacement is a hallmark of amyotrophic lateral sclerosis (ALS), a disease that destroys motor neurons.
- Fields
Neuroscience
Biology
Medicine & Clinical Research
- Topics
TDP-43 proteinopathy
Aggregatin
amyotrophic lateral sclerosis
- Grants
- 1 known grant, through Jul 2031
What they work on
- 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.
- Determine whether Aggregatin drives TDP-43-associated mitochondrial dysfunction through its location in mitochondria, using knockout models.
- Investigate whether Aggregatin, found in both the nucleus and mitochondria, relays stress signals between the two organelles during TDP-43 proteinopathy.
More about the research
It also occurs in frontotemporal dementia, Alzheimer's disease (AD) and related age-related dementias. Faulty TDP-43 disrupts both the nucleus and the mitochondria, the cell's energy producers, and this helps kill neurons. How these two compartments communicate during disease remains poorly understood.
Why it matters
TDP-43 pathology occurs in ALS, frontotemporal dementia, Alzheimer's disease and other age-related dementias that currently lack effective treatments. If Aggregatin proves to control how toxic TDP-43 becomes, it could become a new therapeutic target for these neurodegenerative diseases.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
The school
University of Arizona: 36 labs on PI Pages, $1.0B a year on research, 487 research doctorates a year.
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